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Smart Bioconjugates

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Smart Biomaterials

Abstract

Bioconjugations with synthetic polymers have been a versatile way to add new value, advanced features and unique properties to biomolecules. Smart polymer-protein conjugates have been investigated over the past 30 years. Since the conjugation of smart polymer to single molecule can generate a nano-scale switch, many researchers have conjugated smart polymers to proteins for a great variety of applications in affinity separations, enzyme bioprocesses, drug delivery, diagnostics and biosensors, cell culture processes including tissue engineering, and DNA motors. Biomolecules that can be conjugated with smart polymers include not only proteins but also peptides, polysaccharides, and DNA, and lipids etc. This chapter reviews different types of smart polymer-biomolecule conjugates that have been developed in the last decades.

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References

  1. Ringsdorf H (1975) Structure and properties of pharmacologically active polymers. J Polym Sci: Polym Symp 51:135–153. doi:10.1002/polc.5070510111

    Google Scholar 

  2. Matsumura Y, Maeda H (1986) A new concept for macromolecular therapeutics in cancer chemotherapy: mechanism of tumoritropic accumulation of proteins and the antitumor agent smancs. Cancer Res 46:6387–6392

    Google Scholar 

  3. Abuchowski A, McCoy JR, Palczuk NC, van Es T, Davis FF (1977) Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J Biol Chem 252:3582–3586

    Google Scholar 

  4. Mok H, Palmer DJ, Ng P, Barry MA (2005) Evaluation of polyethylene glycol modification of first-generation and helper-dependent adenoviral vectors to reduce innate immune responses. Mol Ther 11:66–79

    Google Scholar 

  5. O’Riordan CR, Song A (2008) PEGylated adenovirus for targeted gene therapy. In: Doux J (ed) Gene therapy protocols, vol 434. Methods in molecular biology™. Humana Press, pp 133–160. doi:10.1007/978-1-60327-248-3_9

    Google Scholar 

  6. Scott MD, Murad KL, Koumpouras F, Talbot M, Eaton JW (1997) Chemical camouflage of antigenic determinants: Stealth erythrocytes. In: Proceedings of the national academy of sciences, vol 94. U.S.A., pp 7566–7571

    Google Scholar 

  7. Hashemi-Najafabadi S, Vasheghani-Farahani E, Shojaosadati SA, Rasaee MJ, Armstrong JK, Moin M, Pourpak Z (2006) A method to optimize PEG-coating of red blood cells. Bioconjug Chem 17:1288–1293. doi:10.1021/bc060057w

    Google Scholar 

  8. Mansouri S, Merhi Y, Winnik FM, Tabrizian M (2011) Investigation of layer-by-layer assembly of polyelectrolytes on fully functional human red blood cells in suspension for attenuated immune response. Biomacromolecules 12:585–592. doi:10.1021/bm101200c

    Google Scholar 

  9. Charles M, Coughlin RW, Hasselberger FX (1974) Soluble–insoluble enzyme catalysts. Biotechnol Bioeng 16:1553–1556. doi:10.1002/bit.260161113

    Google Scholar 

  10. Van Leemputten E, Horisberger M (1976) Soluble–insoluble complex of trypsin immobilized on acrolein–acrylic acid copolymer. Biotechnol Bioeng 18:587–590. doi:10.1002/bit.260180410

    Google Scholar 

  11. Shoemaker SG, Hoffman AS, Priest JH (1987) Synthesis and properties of vinyl monomer/enzyme conjugates. Appl Biochem Biotechnol 15:11–24. doi:10.1007/bf02798503

    Google Scholar 

  12. Auditore-Hargreaves K, Houghton RL, Monji N, Priest JH, Hoffman AS, Nowinski RC (1987) Phase-separation immunoassays. Clin Chem 33:1509–1516

    Google Scholar 

  13. Hoffman AS (1987) Applications of thermally reversible polymers and hydrogels in therapeutics and diagnostics. J Controlled Release 6:297–305. http://dx.doi.org/10.1016/0168-3659(87)90083-6

    Google Scholar 

  14. Monji N, Hoffman A (1987) A novel immunoassay system and bioseparation process based on thermal phase separating polymers. Appl Biochem Biotechnol 14:107–120. doi:10.1007/bf02798429

    Google Scholar 

  15. Luong JHT, Nguyen A-L (1990) Affinity partitioning of bioproducts. Nat Biotech 8:306–307

    Google Scholar 

  16. Takei YG, Aoki T, Sanui K, Ogata N, Sakurai Y, Okano T, Matsukata M, Kikuchi A (1994) Temperature-responsive bioconjugates. 3. Antibody-poly(N-isopropylacrylamide) conjugates for temperature-modulated precipitations and affinity bioseparations. Bioconjug Chem 5:577–582. doi:10.1021/bc00030a013

    Google Scholar 

  17. Fujimura M, Mori T, Tosa T (1987) Preparation and properties of soluble–insoluble immobilized proteases. Biotechnol Bioeng 29:747–752. doi:10.1002/bit.260290612

    Google Scholar 

  18. Ito Y, Kotoura M, Chung DJ, Imanishi Y (1993) Trypsin modification by vinyl polymers with variable solubilities in response to external signals. Bioconjug Chem 4:358–361. doi:10.1021/bc00023a009

    Google Scholar 

  19. Shimoboji T, Ding ZL, Stayton PS, Hoffman AS (2002) Photoswitching of ligand association with a photoresponsive polymer-protein conjugate. Bioconjug Chem 13:915–919. doi:10.1021/bc010057q

    Google Scholar 

  20. Dainiak MB, Izumrudov VA, Muronetz VI, Galaev IY, Mattiasson B (1998) Conjugates of monoclonal antibodies with polyelectrolyte complexes—an attempt to make an artificial chaperone. Biochim Biophys Acta 1381:279–285. http://dx.doi.org/10.1016/S0304-4165(98)00035-X

  21. Muronetz VI, Kazakov SV, Dainiak MB, Izumrudov VA, Galaev IY, Mattiasson B (2000) Interaction of antibodies and antigens conjugated with synthetic polyanions: on the way of creating an artificial chaperone. Biochim Biophys Acta 1475:141–150. http://dx.doi.org/10.1016/S0304-4165(00)00060-X

    Google Scholar 

  22. Lackey CA, Press OW, Hoffman AS, Stayton PS (2002) A biomimetic pH-responsive polymer directs endosomal release and intracellular delivery of an endocytosed antibody complex. Bioconjug Chem 13:996–1001. doi:10.1021/bc010053l

    Google Scholar 

  23. Furgeson DY, Dreher MR, Chilkoti A (2006) Structural optimization of a “smart” doxorubicin–polypeptide conjugate for thermally targeted delivery to solid tumors. J Controlled Release 110:362–369. http://dx.doi.org/10.1016/j.jconrel.2005.10.006

    Google Scholar 

  24. Golden AL, Battrell CF, Pennell S, Hoffman AS, J. Lai J, Stayton PS (2010) Simple fluidic system for purifying and concentrating diagnostic biomarkers using stimuli-responsive antibody conjugates and membranes. Bioconjug Chem 21:1820–1826. doi:10.1021/bc100169y

    Google Scholar 

  25. Mori T, Maeda M (2003) Temperature-Responsive formation of colloidal nanoparticles from poly(N-isopropylacrylamide) grafted with single-stranded DNA. Langmuir 20:313–319. doi:10.1021/la0356194

    Google Scholar 

  26. Ebara M, Uto K, Idota N, Hoffman JM, Aoyagi T (2012) Shape-memory surface with dynamically tunable nano-geometry activated by body heat. Adv Mater 24:273–278. doi:10.1002/adma.201102181

    Google Scholar 

  27. Kim Y-J, Ebara M, Aoyagi T (2012) A smart nanofiber web that captures and releases cells. Angew Chem Int Ed 51:10537–10541. doi:10.1002/anie.201204139

    Google Scholar 

  28. Kumar A, Kamihira M, Galaev IY, Mattiasson B, Iijima S (2001) Type-specific separation of animal cells in aqueous two-phase systems using antibody conjugates with temperature-sensitive polymers. Biotechnol Bioeng 75:570–580. doi:10.1002/bit.10080

    Google Scholar 

  29. Pennadam S, Firman K, Alexander C, Gorecki D (2004) Protein-polymer nano-machines. Towards synthetic control of biological processes. J Nanobiotechnol 2:8

    Google Scholar 

  30. Pennadam SS, Lavigne MD, Dutta CF, Firman K, Mernagh D, Górecki DC, Alexander C (2004) Control of a multisubunit DNA Motor by a thermoresponsive Polymer Switch. J Am Chem Soc 126:13208–13209. doi:10.1021/ja045275j

    Google Scholar 

  31. Stoica F, Alexander C, Tirelli N, Miller AF, Saiani A (2008) Selective synthesis of double temperature-sensitive polymer-peptide conjugates. Chem Commun 37:4433–4435

    Google Scholar 

  32. Fujimoto K, Iwasaki C, Arai C, Kuwako M, Yasugi E (2000) Control of cell death by the smart polymeric vehicle. Biomacromolecules 1:515–518. doi:10.1021/bm000082j

    Google Scholar 

  33. Vázquez-Dorbatt V, Tolstyka ZP, Maynard HD (2009) Synthesis of aminooxy end-functionalized PNIPAAm by RAFT polymerization for protein and polysaccharide conjugation. Macromolecules 42:7650–7656. doi:10.1021/ma9013803

    Google Scholar 

  34. Lima A, Song W, Blanco-Fernandez B, Alvarez-Lorenzo C, Mano J (2011) Synthesis of temperature-responsive dextran-MA/PNIPAAm particles for controlled drug delivery using superhydrophobic surfaces. Pharm Res 28:1294–1305. doi:10.1007/s11095-011-0380-2

    Google Scholar 

  35. Kotsuchibashi Y, Ebara M, Idota N, Narain R, Aoyagi T (2012) A ‘smart’ approach towards the formation of multifunctional nano-assemblies by simple mixing of block copolymers having a common temperature sensitive segment. Polym Chem-Uk 3:1150–1157

    Google Scholar 

  36. Murata M, Kaku W, Anada T, Sato Y, Kano T, Maeda M, Katayama Y (2003) Novel DNA/polymer conjugate for intelligent antisense reagent with improved nuclease resistance. Bioorg Med Chem Lett 13:3967–3970. http://dx.doi.org/10.1016/j.bmcl.2003.08.062

    Google Scholar 

  37. Ta T, Convertine AJ, Reyes CR, Stayton PS, Porter TM (2010) Thermosensitive liposomes modified with poly(N-isopropylacrylamide-co-propylacrylic acid) copolymers for triggered release of doxorubicin. Biomacromolecules 11:1915–1920. doi:10.1021/bm1004993

    Google Scholar 

  38. Kono K, Nakai R, Morimoto K, Takagishi T (1999) Thermosensitive polymer-modified liposomes that release contents around physiological temperature. Biochim Biophys Acta 1416:239–250. http://dx.doi.org/10.1016/S0005-2736(98)00226-0

    Google Scholar 

  39. Stayton PS, Shimoboji T, Long C, Chilkoti A, Ghen G, Harris JM, Hoffman AS (1995) Control of protein-ligand recognition using a stimuli-responsive polymer. Nature 378:472–474

    Google Scholar 

  40. Kiick KL, Tirrell DA (2000) Protein engineering by in vivo incorporation of non-natural amino acids: control of incorporation of methionine analogues by methionyl-trna synthetase. Tetrahedron 56:9487-9493. http://dx.doi.org/10.1016/S0040-4020(00)00833-4

    Google Scholar 

  41. Chen J-P, Chu D-H, Sun Y-M (1997) Immobilization of α-amylase to temperature-responsive polymers by single or multiple point attachments. J Chem Technol Biotechnol 69:421–428. doi:10.1002/(sici)1097-4660(199708)69:4<421:aid-jctb730>3.0.co;2-3

    Google Scholar 

  42. Matsukata M, Aoki T, Sanui K, Ogata N, Kikuchi A, Sakurai Y, Okano T (1996) Effect of molecular architecture of poly(N-isopropylacrylamide)–trypsin conjugates on their solution and enzymatic properties. Bioconjug Chem 7:96–101. doi:10.1021/bc950082u

    Google Scholar 

  43. Chen G, Hoffman AS (1993) Preparation and properties of thermoreversible, phase-separating enzyme-oligo (N-isopropylacrylamide) conjugates. Bioconjug Chem 4:509–514. doi:10.1021/bc00024a013

    Google Scholar 

  44. Plourde R, Phillips AT, Wu CH, Hays RM, Chowdhury JR, Chowdhury NR, Wu GY (1996) A hepatocyte-targeted conjugate capable of delivering biologically active colchicine in vitro. Bioconjug Chem 7:131–137. doi:10.1021/bc950083m

    Google Scholar 

  45. Chiefari J, Chong YK, Ercole F, Kristina J, Jeffery J, Le TPT, Mayadunne RTA, Meijs GF, Moad CL, Moad G, Rizzardo E, Thang SH (1998) Living free-radical polymerization by reversible addition—fragmentation chain transfer: the RAFT process. Macromolecules 31:5559–5562. doi:10.1021/ma9804951

    Google Scholar 

  46. Lele BS, Murata H, Matyjaszewski K, Russell AJ (2005) Synthesis of uniform protein-polymer conjugates. Biomacromolecules 6:3380–3387. doi:10.1021/bm050428w

    Google Scholar 

  47. Lecolley F, Tao L, Mantovani G, Durkin I, Lautru S, Haddleton DM (2004) A new approach to bioconjugates for proteins and peptides (“pegylation”) utilising living radical polymerisation. Chem Commun 0:2026–2027

    Google Scholar 

  48. Tao L, Mantovani G, Lecolley F, Haddleton DM (2004) α-Aldehyde terminally functional methacrylic polymers from living radical polymerization: application in protein conjugation “pegylation”. J Am Chem Soc 126:13220–13221. doi:10.1021/ja0456454

    Google Scholar 

  49. Kulkarni S, Schilli C, Grin B, Müller AHE, Hoffman AS, Stayton PS (2006) Controlling the aggregation of conjugates of streptavidin with smart block copolymers prepared via the RAFT copolymerization technique. Biomacromolecules 7:2736–2741. doi:10.1021/bm060186f

    Google Scholar 

  50. Ding Z, Fong RB, Long CJ, Stayton PS, Hoffman AS (2001) Size-dependent control of the binding of biotinylated proteins to streptavidin using a polymer shield. Nature 411:59–62

    Google Scholar 

  51. Bulmus V, Woodward M, Lin L, Murthy N, Stayton P, Hoffman A (2003) A new pH-responsive and glutathione-reactive, endosomal membrane-disruptive polymeric carrier for intracellular delivery of biomolecular drugs. J Controlled Release 93:105–120. http://dx.doi.org/10.1016/j.jconrel.2003.06.001

    Google Scholar 

  52. Stayton PS, Hoffman AS, El-Sayed M, Kulkarni S, Shimoboji T, Murthy N, Bulmus V, Lackey C (2005) Intelligent biohybrid materials for therapeutic and imaging agent delivery. Proc IEEE 93:726–736. doi:10.1109/jproc.2005.844619

    Google Scholar 

  53. Krishnamurthy VM, Semetey V, Bracher PJ, Shen N, Whitesides GM (2007) Dependence of effective molarity on linker length for an intramolecular protein–ligand system. J Am Chem Soc 129:1312–1320. doi:10.1021/ja066780e

    Google Scholar 

  54. Chilkoti A, Chen G, Stayton PS, Hoffman AS (1994) Site-specific conjugation of a temperature-sensitive polymer to a genetically engineered protein. Bioconjug Chem 5:504–507. doi:10.1021/bc00030a004

    Google Scholar 

  55. Shimoboji T, Larenas E, Fowler T, Kulkarni S, Hoffman AS, Stayton PS (2002) Photoresponsive polymer–enzyme switches. Proc Natl Acad Sci 99:16592–16596. doi:10.1073/pnas.262427799

    Google Scholar 

  56. Bontempo D, Heredia KL, Fish BA, Maynard HD (2004) Cysteine-reactive polymers synthesized by atom transfer radical polymerization for conjugation to proteins. J Am Chem Soc 126:15372–15373. doi:10.1021/ja045063m

    Google Scholar 

  57. Mantovani G, Lecolley F, Tao L, Haddleton DM, Clerx J, Cornelissen JJLM, Velonia K (2005) Design and synthesis of N-maleimido-functionalized hydrophilic polymers via copper-mediated living radical polymerization: a suitable alternative to PEGylation chemistry. J Am Chem Soc 127:2966–2973. doi:10.1021/ja0430999

    Google Scholar 

  58. Geoghegan KF, Stroh JG (1992) Site-directed conjugation of nonpeptide groups to peptides and proteins via periodate oxidation of a 2-amino alcohol. Application to modification at N-terminal serine. Bioconjug Chem 3:138–146. doi:10.1021/bc00014a008

    Google Scholar 

  59. Gaertner HF, Offord RE, Cotton R, Timms D, Camble R, Rose K (1994) Chemo-enzymic backbone engineering of proteins. Site-specific incorporation of synthetic peptides that mimic the 64-74 disulfide loop of granulocyte colony-stimulating factor. J Biol Chem 269:7224–7230

    Google Scholar 

  60. Alouani S, Gaertner HF, Mermod J-J, Power CA, Bacon KB, Wells TNC, Proudfoot AEI (1995) A fluorescent interleukin-8 receptor probe produced by targetted labelling at the amino terminus. Eur J Biochem 227:328–334. doi:10.1111/j.1432-1033.1995.tb20393.x

    Google Scholar 

  61. Gaertner HF, Offord RE (1996) Site-specific attachment of functionalized poly (ethylene glycol) to the amino terminus of proteins. Bioconjug Chem 7:38–44. doi:10.1021/bc950074d

    Google Scholar 

  62. Heredia KL, Bontempo D, Ly T, Byers JT, Halstenberg S, Maynard HD (2005) In situ preparation of protein—“smart” polymer conjugates with retention of bioactivity. J Am Chem Soc 127:16955–16960. doi:10.1021/ja054482w

    Google Scholar 

  63. Bontempo D, Maynard HD (2005) Streptavidin as a macroinitiator for polymerization. In Situ protein-polymer conjugate formation. J Am Chem Soc 127:6508–6509. doi:10.1021/ja042230+

    Google Scholar 

  64. Le Droumaguet B, Velonia K (2008) In Situ ATRP-mediated hierarchical formation of giant amphiphile bionanoreactors. Angew Chem Int Ed 47:6263–6266. doi:10.1002/anie.200801007

    Google Scholar 

  65. Depp V, Alikhani A, Grammer V, Lele BS (2009) Native protein-initiated ATRP: a viable and potentially superior alternative to PEGylation for stabilizing biologics. Acta Biomater 5:560–569. http://dx.doi.org/10.1016/j.actbio.2008.08.010

    Google Scholar 

  66. Magnusson JP, Bersani S, Salmaso S, Alexander C, Caliceti P (2010) In situ growth of side-chain PEG polymers from functionalized human growth hormone—a new technique for preparation of enhanced protein-polymer conjugates. Bioconjugate Chem 21:671–678. doi:10.1021/bc900468v

    Google Scholar 

  67. Gao W, Liu W, Mackay JA, Zalutsky MR, Toone EJ, Chilkoti A (2009) In situ growth of a stoichiometric PEG-like conjugate at a protein’s N-terminus with significantly improved pharmacokinetics. Proc Natl Acad Sci 106:15231–15236. doi:10.1073/pnas.0904378106

    Google Scholar 

  68. Gao W, Liu W, Christensen T, Zalutsky MR, Chilkoti A (2010) In situ growth of a PEG-like polymer from the C terminus of an intein fusion protein improves pharmacokinetics and tumor accumulation. Proc Natl Acad Sci. doi:10.1073/pnas.1006044107

    Google Scholar 

  69. Li H, Li M, Yu X, Bapat AP, Sumerlin BS (2011) Block copolymer conjugates prepared by sequentially grafting from proteins via RAFT. Polym Chem Uk 2:1531–1535

    Google Scholar 

  70. De P, Li M, Gondi SR, Sumerlin BS (2008) Temperature-regulated activity of responsive polymer-protein conjugates prepared by grafting-from via RAFT polymerization. J Am Chem Soc 130:11288–11289. doi:10.1021/ja804495v

    Google Scholar 

  71. Hong C-Y, Pan C-Y (2006) Direct synthesis of biotinylated stimuli-responsive polymer and diblock copolymer by RAFT polymerization using biotinylated trithiocarbonate as RAFT agent. Macromolecules 39:3517–3524. doi:10.1021/ma052593+

    Google Scholar 

  72. Liu J, Bulmus V, Herlambang DL, Barner-Kowollik C, Stenzel MH, Davis TP (2007) In situ formation of protein-polymer conjugates through reversible addition fragmentation chain transfer polymerization. Angew Chem Int Ed 46:3099–3103. doi:10.1002/anie.200604922

    Google Scholar 

  73. Hohsaka T, Sisido M (2002) Incorporation of non-natural amino acids into proteins. Curr Opin Chem Biol 6:809–815. http://dx.doi.org/10.1016/S1367-5931(02)00376-9

    Google Scholar 

  74. Katti KS, Ambre AH, Peterka N, Katti DR (2010) Use of unnatural amino acids for design of novel organomodified clays as components of nanocomposite biomaterials. Philoso Trans R Soc A 368:1963–1980. doi:10.1098/rsta.2010.0008

    Google Scholar 

  75. Dieterich DC, Link AJ, Graumann J, Tirrell DA, Schuman EM (2006) Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT). Proc Natl Acad Sci 103:9482–9487. doi:10.1073/pnas.0601637103

    Google Scholar 

  76. Kolb HC, Finn MG, Sharpless KB (2001) Click chemistry: diverse chemical function from a few good reactions. Angew Chem Int Ed 40:2004–2021. doi:10.1002/1521-3773(20010601)40:11<2004:aid-anie2004>3.0.co;2-5

    Google Scholar 

  77. Peeler JC, Woodman BF, Averick S, Miyake-Stoner SJ, Stokes AL, Hess KR, Matyjaszewski K, Mehl RA (2010) Genetically encoded initiator for polymer growth from proteins. J Am Chem Soc 132:13575–13577. doi:10.1021/ja104493d

    Google Scholar 

  78. Averick SE, Magenau AJD, Simakova A, Woodman BF, Seong A, Mehl RA, Matyjaszewski K (2011) Covalently incorporated protein-nanogels using AGET ATRP in an inverse miniemulsion. Polym Chem-Uk 2:1476–1478

    Google Scholar 

  79. Kulkarni S, Schilli C, Müller AHE, Hoffman AS, Stayton PS (2004) Reversible meso-scale smart polymer-protein particles of controlled sizes. Bioconjugate Chem 15:747–753. doi:10.1021/bc034215k

    Google Scholar 

  80. Hoffman JM, Ebara M, Lai JJ, Hoffman AS, Folch A, Stayton PS (2010) A helical flow, circular microreactor for separating and enriching “smart” polymer-antibody capture reagents. Lab Chip 10:3130–3138

    Google Scholar 

  81. Hannink JM, Cornelissen JJLM, Farrera JA, Foubert P, De Schryver FC, Sommerdijk NAJM, Nolte RJM (2001) Protein-polymer hybrid amphiphiles. Angew Chem Int Ed 40:4732–4734. doi:10.1002/1521-3773(20011217)40:24<4732:aid-anie4732>3.0.co;2-p

    Google Scholar 

  82. Boerakker MJ, Hannink JM, Bomans PHH, Frederik PM, Nolte RJM, Meijer EM, Sommerdijk NAJM (2002) Giant amphiphiles by cofactor reconstitution. Angew Chem Int Ed 41:4239–4241. doi:10.1002/1521-3773(20021115)41:22<4239:aid-anie4239>3.0.co;2-e

    Google Scholar 

  83. Sun X-L, Faucher KM, Houston M, Grande D, Chaikof EL (2002) Design and synthesis of biotin chain-terminated glycopolymers for surface glycoengineering. J Am Chem Soc 124:7258–7259. doi:10.1021/ja025788v

    Google Scholar 

  84. Hou S, Sun X-L, Dong C-M, Chaikof EL (2004) Facile synthesis of chain-end functionalized glycopolymers for site-specific bioconjugation. Bioconjug Chem 15:954–959. doi:10.1021/bc0499275

    Google Scholar 

  85. Bontempo D, Li RC, Ly T, Brubaker CE, Maynard HD (2005) One-step synthesis of low polydispersity, biotinylated poly(N-isopropylacrylamide) by ATRP. Chem Commun 0:4702–4704

    Google Scholar 

  86. Kopping JT, Tolstyka ZP, Maynard HD (2007) Telechelic aminooxy polystyrene synthesized by ATRP and ATR coupling. Macromolecules 40:8593–8599. doi:10.1021/ma071606b

    Google Scholar 

  87. Tolstyka ZP, Kopping JT, Maynard HD (2007) Straightforward synthesis of cysteine-reactive telechelic polystyrene. Macromolecules 41:599–606. doi:10.1021/ma702161q

    Google Scholar 

  88. Tao L, Kaddis CS, Ogorzalek Loo RR, Grover GN, Loo JA, Maynard HD (2009) Synthetic approach to homodimeric protein–polymer conjugates. Chem Commun 0:2148–2150

    Google Scholar 

  89. Tao L, Kaddis CS, Loo RRO, Grover GN, Loo JA, Maynard HD (2009) Synthesis of maleimide-end-functionalized star polymers and multimeric protein-polymer conjugates. Macromolecules 42:8028–8033. doi:10.1021/ma901540p

    Google Scholar 

  90. Boyer C, Liu J, Bulmus V, Davis TP, Barner-Kowollik C, Stenzel MH (2008) Direct synthesis of well-defined heterotelechelic polymers for bioconjugations. Macromolecules 41:5641–5650. doi:10.1021/ma800289u

    Google Scholar 

  91. Heredia KL, Grover GN, Tao L, Maynard HD (2009) Synthesis of heterotelechelic polymers for conjugation of two different proteins. Macromolecules 42:2360–2367. doi:10.1021/ma8022712

    Google Scholar 

  92. Heredia KL, Tao L, Grover GN, Maynard HD (2010) Heterotelechelic polymers for capture and release of protein-polymer conjugates. Polym Chem-Uk 1:168–170

    Google Scholar 

  93. Yoshimoto T, Takahashi K, Ajima A, Matsushima A, Saito Y, Tamaura Y, Inada Y (1985) Activation and stabilization of asparaginase by anti-asparaginase IgG and its Fab. FEBS Lett 183:170–172. http://dx.doi.org/10.1016/0014-5793(85)80978-9

    Google Scholar 

  94. Zhang Y-Q, Tao M-L, Shen W-D, Mao J-P, Chen Y-h (2006) Synthesis of silk sericin peptides–L-asparaginase bioconjugates and their characterization. J Chem Technol Biotechnol 81:136–145. doi:10.1002/jctb.1370

    Google Scholar 

  95. Xia F, Zuo X, Yang R, Xiao Y, Kang D, Vallée-Bélisle A, Gong X, Heeger AJ, Plaxco KW (2010) On the binding of cationic, water-soluble conjugated polymers to DNA: electrostatic and hydrophobic interactions. J Am Chem Soc 132:1252–1254. doi:10.1021/ja908890q

    Google Scholar 

  96. Decher G (1997) Fuzzy nanoassemblies: toward layered polymeric multicomposites. Science 277:1232–1237. doi:10.1126/science.277.5330.1232

    Google Scholar 

  97. Okada T, Uto K, Sasai M, Lee CM, Ebara M, Aoyagi T (2013) Nano-decoration of Hemagglutinating Virus of Japan Envelope (HVJ-E) using Layer-by-Layer Assembly Technique. Langmuir 29:7384–7392. doi:10.1021/la304572s

    Google Scholar 

  98. Carlos Rodríguez-Cabello J, Reguera J, Girotti A, Alonso M, Testera AM (2005) Developing functionality in elastin-like polymers by increasing their molecular complexity: the power of the genetic engineering approach. Prog Polym Sci 30:1119–1145. http://dx.doi.org/10.1016/j.progpolymsci.2005.07.004

  99. Urry DW (2004) The change in Gibbs free energy for hydrophobic association: derivation and evaluation by means of inverse temperature transitions. Chem Phys Lett 399:177–183. http://dx.doi.org/10.1016/j.cplett.2004.09.137

    Google Scholar 

  100. Meyer DE, Kong GA, Dewhirst MW, Zalutsky MR, Chilkoti A (2001) Targeting a genetically engineered elastin-like polypeptide to solid tumors by local hyperthermia. Cancer Res 61:1548–1554

    Google Scholar 

  101. Kostal J, Mulchandani A, Chen W (2001) Tunable biopolymers for heavy metal removal. Macromolecules 34:2257–2261. doi:10.1021/ma001973m

    Google Scholar 

  102. Wan X, Zhang G, Ge Z, Narain R, Liu S (2011) Construction of polymer-protein bioconjugates with varying chain topologies: polymer molecular weight and steric hindrance effects. Chem Asian J 6:2835-2845. doi:10.1002/asia.201100489

    Google Scholar 

  103. Yan M, Ge J, Dong W, Liu Z, Ouyang P (2006) Preparation and characterization of a temperature-sensitive sulfobetaine polymer–trypsin conjugate. Biochem Eng J 30:48–54. http://dx.doi.org/10.1016/j.bej.2006.02.001

    Google Scholar 

  104. Sharma S, Kaur P, Jain A, Rajeswari MR, Gupta MN (2003) A smart bioconjugate of chymotrypsin. Biomacromolecules 4:330–336. doi:10.1021/bm0256799

    Google Scholar 

  105. Pan LC, Chien CC (2003) A novel application of thermo-responsive polymer to affinity precipitation of polysaccharide. J Biochem Bioph Methods 55:87–94. http://dx.doi.org/10.1016/S0165-022X(02)00180-X

    Google Scholar 

  106. Anastase-Ravion S, Ding Z, Pellé A, Hoffman AS, Letourneur D (2001) New antibody purification procedure using a thermally responsive poly(N-isopropylacrylamide)–dextran derivative conjugate. J Chromatogr B: Biomed Sci Appl 761:247–254. http://dx.doi.org/10.1016/S0378-4347(01)00336-X

    Google Scholar 

  107. Chang C-W, Nguyen TH, Maynard HD (2010) Thermoprecipitation of glutathione S-transferase by glutathione–poly(N-isopropylacrylamide) Prepared by RAFT Polymerization. Macromol Rapid Commun 31:1691–1695. doi:10.1002/marc.201000333

    Google Scholar 

  108. Mattiasson B, Kumar A, Galaev IY (1998) Affinity precipitation of proteins: design criteria for an efficient polymer. J Mol Recognit 11:211–216. doi:10.1002/(sici)1099-1352(199812)11:1/6<211:aid-jmr425>3.0.co;2-y

    Google Scholar 

  109. Galaev IY, Mattiasson B (1993) Affinity thermoprecipitation: contribution of the efficiency of ligand–protein interaction and access of the ligand. Biotechnol Bioeng 41:1101–1106. doi:10.1002/bit.260411113

    Google Scholar 

  110. Kumar A, Srivastava A, Galaev IY, Mattiasson B (2007) Smart polymers: physical forms and bioengineering applications. Prog Polym Sci 32:1205–1237. http://dx.doi.org/10.1016/j.progpolymsci.2007.05.003

    Google Scholar 

  111. Kumar A, Wahlund P-O, Kepka C, Galaev IY, Mattiasson B (2003) Purification of histidine-tagged single-chain Fv-antibody fragments by metal chelate affinity precipitation using thermoresponsive copolymers. Biotechnol Bioeng 84:494–503. doi:10.1002/bit.10810

    Google Scholar 

  112. Balan S, Murphy J, Galaev I, Kumar A, Fox G, Mattiasson B, Willson R (2003) Metal chelate affinity precipitation of RNA and purification of plasmid DNA. Biotechnol Lett 25:1111–1116. doi:10.1023/a:1024148316322

    Google Scholar 

  113. Murphy JC, Jewell DL, White KI, Fox GE, Willson RC (2003) Nucleic Acid Separations Utilizing Immobilized Metal Affinity Chromatography. Biotechnol Progr 19:982–986. doi:10.1021/bp025563o

    Google Scholar 

  114. Ding Z, Long CJ, Hayashi Y, Bulmus EV, Hoffman AS, Stayton PS (1999) Temperature control of biotin binding and release with a streptavidin-poly(N-isopropylacrylamide) site-specific conjugate. Bioconjug Chem 10:395–400. doi:10.1021/bc980108s

    Google Scholar 

  115. Bulmus V, Ding Z, Long CJ, Stayton PS, Hoffman AS (1999) Site-specific polymer–streptavidin bioconjugate for ph-controlled binding and triggered release of biotin. Bioconjug Chem 11:78–83. doi:10.1021/bc9901043

    Google Scholar 

  116. Shimoboji T, Ding Z, Stayton PS, Hoffman AS (2001) Mechanistic investigation of smart polymer-protein conjugates. Bioconjug Chem 12:314–319. doi:10.1021/bc000107b

    Google Scholar 

  117. Shimoboji T, Larenas E, Fowler T, Hoffman AS, Stayton PS (2003) Temperature-induced switching of enzyme activity with smart polymer–enzyme conjugates. Bioconjug Chem 14:517–525. doi:10.1021/bc025615v

    Google Scholar 

  118. Hohsaka T, Kawashima K, Sisido M (1994) Photoswitching of NAD+-mediated enzyme reaction through photoreversible antigen-antibody reaction. J Am Chem Soc 116:413–414. doi:10.1021/ja00080a064

    Google Scholar 

  119. Murata M, Kaku W, Anada T, Soh N, Katayama Y, Maeda M (2003) Thermoresponsive DNA/polymer conjugate for intelligent antisense strategy. Chem Lett 32:266–267

    Google Scholar 

  120. Lackey CA, Murthy N, Press OW, Tirrell DA, Hoffman AS, Stayton PS (1999) Hemolytic activity of pH-responsive polymer-streptavidin bioconjugates. Bioconjugate Chem 10:401–405. doi:10.1021/bc980109k

    Google Scholar 

  121. Jones RA, Cheung CY, Black FE, Zia JK, Stayton PS, Hoffman AS, Wilson MR (2003) Poly(2-alkylacrylic acid) polymers deliver molecules to the cytosol by pH-sensitive disruption of endosomal vesicles. Biochem J 372:65–75. doi:10.1042/bj20021945

    Google Scholar 

  122. Kyriakides TR, Cheung CY, Murthy N, Bornstein P, Stayton PS, Hoffman AS (2002) pH-Sensitive polymers that enhance intracellular drug delivery in vivo. J Controlled Release 78:295–303. http://dx.doi.org/10.1016/S0168-3659(01)00504-1

    Google Scholar 

  123. Berguig GY, Convertine AJ, Shi J, Palanca-Wessels MC, Duvall CL, Pun SH, Press OW, Stayton PS (2012) Intracellular delivery and trafficking dynamics of a lymphoma-targeting antibody-polymer conjugate. Mol Pharm 9:3506–3514. doi:10.1021/mp300338s

    Google Scholar 

  124. Dubé D, Francis M, Leroux J-C, Winnik FM (2002) Preparation and Tumor Cell Uptake of Poly(N-isopropylacrylamide) Folate Conjugates. Bioconjugate Chem 13:685–692. doi:10.1021/bc010084g

    Google Scholar 

  125. Benoit DSW, Srinivasan S, Shubin AD, Stayton PS (2011) Synthesis of Folate-Functionalized RAFT Polymers for Targeted siRNA Delivery. Biomacromolecules 12:2708–2714. doi:10.1021/bm200485b

    Google Scholar 

  126. Flanary S, Hoffman AS, Stayton PS (2009) Antigen delivery with poly(Propylacrylic acid) conjugation enhances MHC-1 presentation and t-cell activation. Bioconjug Chem 20:241–248. doi:10.1021/bc800317a

    Google Scholar 

  127. Foster S, Duvall CL, Crownover EF, Hoffman AS, Stayton PS (2010) Intracellular delivery of a protein antigen with an endosomal-releasing polymer enhances cd8 t-cell production and prophylactic vaccine efficacy. Bioconjug Chem 21:2205–2212. doi:10.1021/bc100204m

    Google Scholar 

  128. Albarran B, Hoffman AS, Stayton PS (2011) Efficient intracellular delivery of a pro-apoptotic peptide with a pH-responsive carrier. React Funct Polym 71:261–265. http://dx.doi.org/10.1016/j.reactfunctpolym.2010.09.008

    Google Scholar 

  129. Napoli A, Valentini M, Tirelli N, Muller M, Hubbell JA (2004) Oxidation-responsive polymeric vesicles. Nat Mater 3:183–189. http://www.nature.com/nmat/journal/v3/n3/suppinfo/nmat1081_S1.html

    Google Scholar 

  130. El-Sayed MEH, Hoffman AS, Stayton PS (2005) Rational design of composition and activity correlations for pH-sensitive and glutathione-reactive polymer therapeutics. J Controlled Release 101:47–58. http://dx.doi.org/10.1016/j.jconrel.2004.08.032

  131. Manickam DS, Oupický D (2006) Multiblock reducible copolypeptides containing histidine-rich and nuclear localization sequences for gene delivery. Bioconjug Chem 17:1395–1403. doi:10.1021/bc060104k

    Google Scholar 

  132. Raucher D, Chilkoti A (2001) Enhanced Uptake of a Thermally Responsive Polypeptide by Tumor Cells in Response to Its Hyperthermia-mediated Phase Transition. Cancer Res 61:7163–7170

    Google Scholar 

  133. Agasti SS, Liong M, Peterson VM, Lee H, Weissleder R (2012) Photocleavable DNA barcode-antibody conjugates allow sensitive and multiplexed protein analysis in single cells. J Am Chem Soc 134:18499–18502. doi:10.1021/ja307689w

    Google Scholar 

  134. Maeda M (2006) Sequence-specific aggregation behavior of DNA-carrying colloidal nanoparticles prepared from poly(N-isopropylacrylamide)-graft-oligodeoxyribonucleotide. Polym J 38:1099–1104

    Google Scholar 

  135. Mori T, Maeda M (2001) Formation of DNA-carrying colloidal particle from poly(N-isopropylacrylamide)-graft-DNA copolymer and its assembly through hybridization. Polym J 33:830

    Google Scholar 

  136. Mori T, Maeda M (2002) Stability change of DNA-carrying colloidal particle induced by hybridization with target DNA. Polym J 34:624

    Google Scholar 

  137. Marie Dupuy A, Lehmann S, Paul Cristol J (2005) Protein biochip systems for the clinical laboratory. Clin Chem Lab Med 43:1291–1302. doi:10.1515/cclm.2005.223

  138. Toner M, Irimia D (2005) Blood-on-a-Chip. Annu Rev Biomed Eng 7:77–103. doi:10.1146/annurev.bioeng.7.011205.135108

    Google Scholar 

  139. Malmstadt N, Hoffman AS, Stayton PS (2004) “Smart” mobile affinity matrix for microfluidic immunoassays. Lab Chip 4:412–415

    Google Scholar 

  140. Malmstadt N, Yager P, Hoffman AS, Stayton PS (2003) A smart microfluidic affinity chromatography matrix composed of poly(N-isopropylacrylamide)-coated beads. Anal Chem 75:2943–2949. doi:10.1021/ac034274r

    Google Scholar 

  141. Ebara M, Hoffman JM, Hoffman AS, Stayton PS (2006) Switchable surface traps for injectable bead-based chromatography in PDMS microfluidic channels. Lab Chip 6:843–848

    Google Scholar 

  142. Ebara M, Hoffman JM, Stayton PS, Hoffman AS (2007) Surface modification of microfluidic channels by UV-mediated graft polymerization of non-fouling and ‘smart’ polymers. Radiat Phys Chem 76:1409–1413. http://dx.doi.org/10.1016/j.radphyschem.2007.02.072

    Google Scholar 

  143. Ebara M, Hoffman AS, Stayton PS, Lai JJ (2013) A photo-induced nanoparticle separation in microchannels via pH-sensitive surface traps. Langmuir 29:5388–5393. doi:10.1021/la400347r

    Google Scholar 

  144. Lai JJ, Hoffman JM, Ebara M, Hoffman AS, Estournès C, Wattiaux A, Stayton PS (2007) Dual magnetic-/temperature-responsive nanoparticles for microfluidic separations and assays. Langmuir 23:7385–7391. doi:10.1021/la062527g

    Google Scholar 

  145. Lai JJ, Nelson KE, Nash MA, Hoffman AS, Yager P, Stayton PS (2009) Dynamic bioprocessing and microfluidic transport control with smart magnetic nanoparticles in laminar-flow devices. Lab Chip 9:1997–2002

    Google Scholar 

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Correspondence to Mitsuhiro Ebara or John M. Hoffman .

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© 2014 National Institute for Materials Science, Japan. Published by Springer Japan

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Ebara, M. et al. (2014). Smart Bioconjugates. In: Smart Biomaterials. NIMS Monographs. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54400-5_6

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