Biological Trace Element Research

, Volume 146, Issue 3, pp 396–401 | Cite as

The Interactions of Glutathione-Capped CdTe Quantum Dots with Trypsin

  • Bingjun Yang
  • Rutao Liu
  • Xiaopeng Hao
  • Yongzhong Wu
  • Jie Du
Article

Abstract

Due to their unique fluorescent properties, quantum dots present a great potential for biolabelling applications; however, the toxic interactions of quantum dots with biopolymers are little known. The toxic interactions of glutathione-capped CdTe quantum dots with trypsin were studied in this paper using synchronous fluorescence spectroscopy, fluorescence emission spectra, and UV–vis absorption spectra. The interaction between CdTe quantum dots and trypsin resulted in structure changes of trypsin and inhibited trypsin's activity. Fluorescence emission spectra revealed that the quenching mechanism of trypsin by CdTe quantum dots was a static quenching process. The binding constant and the number of binding sites at 288 and 298 K were calculated to be 1.98 × 106 L mol−1 and 1.37, and 6.43 × 104 L mol−1 and 1.09, respectively. Hydrogen bonds and van der Waals' forces played major roles in this process.

Keywords

Quantum dots Trypsin Toxic interaction Multi-spectroscopic techniques Fluorescence spectroscopy 

References

  1. 1.
    Weng JF, Song XT, Li LA et al (2006) Highly luminescent CdTe quantum dots prepared in aqueous phase as an alternative fluorescent probe for cell imaging. Talanta 2:397–402CrossRefGoogle Scholar
  2. 2.
    Medintz IL, Uyeda HT, Goldman ER et al (2005) Quantum dot bioconjugates for imaging, labelling and sensing. Nat Mater 6:435–446CrossRefGoogle Scholar
  3. 3.
    Jamieson T, Bakhshi R, Petrova D et al (2007) Biological applications of quantum dots. Biomaterials 31:4717–4732CrossRefGoogle Scholar
  4. 4.
    Rehberg M, Praetner M, Leite CF et al (2010) Quantum dots modulate leukocyte adhesion and transmigration depending on their surface modification. Nano Lett 9:3656–3664CrossRefGoogle Scholar
  5. 5.
    Shiohara A, Hoshino A, Hanaki K et al (2004) On the cyto-toxicity caused by quantum dots. Microbiol Immunol 9:669–675Google Scholar
  6. 6.
    Lovric J, Bazzi HS, Cuie Y et al (2005) Differences in subcellular distribution and toxicity of green and red emitting CdTe quantum dots. J Mol Med-Jmm 5:377–385CrossRefGoogle Scholar
  7. 7.
    Hardman R (2006) A toxicologic review of quantum dots: toxicity depends on physicochemical and environmental factors. Environ Health Persp 2:165–172CrossRefGoogle Scholar
  8. 8.
    Zhao LZ, Liu RT, Zhao XC et al (2009) New strategy for the evaluation of CdTe quantum dot toxicity targeted to bovine serum albumin. Sci Total Environ 18:5019–5023Google Scholar
  9. 9.
    Ghosh S, Banerjee A (2002) A multitechnique approach in protein/surfactant interaction study: physicochemical aspects of sodium dodecyl sulfate in the presence of trypsin in aqueous medium. Biomacromolecules 1:9–16CrossRefGoogle Scholar
  10. 10.
    Huang YB, Liu BZ, Yu Z et al (2010) Luminescence quenching effect for the interaction of prulifloxacin with trypsin-Britton-Robinson buffer solution system. J Lumin 3:360–364CrossRefGoogle Scholar
  11. 11.
    Zhang HM, Zhou QH, Wang YQ (2010) Studies on the interactions of 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin. J Fluoresc 2:507–516CrossRefGoogle Scholar
  12. 12.
    Jingzhou F (2010) Multi–spectroscopic study on the interaction between CdTe quantum dots and bovine serum albumin. Chin J Chem 28:2353–2358CrossRefGoogle Scholar
  13. 13.
    Shi L, Rosenzweig N, Rosenzweig Z (2007) Luminescent quantum dots fluorescence resonance energy transfer-based probes for enzymatic activity and enzyme inhibitors. Anal Chem 1:208–214CrossRefGoogle Scholar
  14. 14.
    Blanco-Canosa JB, Medintz IL, Farrell D et al (2010) Rapid covalent ligation of fluorescent peptides to water solubilized quantum dots. J Am Chem Soc 29:10027–10033CrossRefGoogle Scholar
  15. 15.
    Wang L, Gong HB, Lv RJ et al (2010) A one-pot aqueous synthesis of high-luminescent thiol-capped CdTe and its bioapplication. J Nanosci Nanotechnol 10:1–5CrossRefGoogle Scholar
  16. 16.
    Schwert GW, Takenaka Y (1955) A spectrophotometric determination of trypsin and chymotrypsin. Biochim Biophys Acta 16:570–575PubMedCrossRefGoogle Scholar
  17. 17.
    Stellmach B (1988) Trypsin. In: Qian JY (ed) The methods of enzyme activity determination, Chinese edition. China Light Industry Press, BeijingGoogle Scholar
  18. 18.
    Marrakchi M, Dzyadevych SV, Biloivan OA et al (2006) Development of trypsin biosensor based on ion sensitive field-effect transistors for proteins determination. Mat Sci Eng C-Bio Syst 2–3:369–373CrossRefGoogle Scholar
  19. 19.
    Koutsopoulos S, Patzsch K, Bosker WTE et al (2007) Adsorption of trypsin on hydrophilic and hydrophobic surfaces. Langmuir 4:2000–2006CrossRefGoogle Scholar
  20. 20.
    Bowen S, Hilty C (2008) Time-resolved dynamic nuclear polarization enhanced NMR spectroscopy. Angew Chem Int Edit 28:5235–5237Google Scholar
  21. 21.
    Yu YQ, Gilar M, Lee PJ et al (2003) Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins. Anal Chem 21:6023–6028CrossRefGoogle Scholar
  22. 22.
    Zhao XC, Liu RT, Chi ZX et al (2010) New insights into the behavior of bovine serum albumin adsorbed onto carbon nanotubes: comprehensive spectroscopic studies. J Phys Chem B 16:5625–5631CrossRefGoogle Scholar
  23. 23.
    Rk S (1974) Measurement of protein by spectrophotometry at 205 nm. Anal Biochem 1:277–282Google Scholar
  24. 24.
    Aitken A, Learmonth M (1996) Protein determination by UV absorption. In: Walker JM (ed) The protein protocols handbook, 2nd edn. Humana Press Inc., Totowa, pp 3–6CrossRefGoogle Scholar
  25. 25.
    Beaven GH, Holiday ER (1952) Ultraviolet absorption spectra of proteins and amino acids. Adv Protein Chem 7:319–386PubMedCrossRefGoogle Scholar
  26. 26.
    Edelhoch H (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochem 7:1948–1954Google Scholar
  27. 27.
    Pace CN, Vajdos F, Fee L et al (1995) How to measure and predict the molar absorption coefficient of a protein. Prot Sci 11:2411–2423CrossRefGoogle Scholar
  28. 28.
    Chi ZX, Liu RT, Zhang H (2010) Noncovalent interaction of oxytetracycline with the enzyme trypsin. Biomacromolecules 9:2454–2459CrossRefGoogle Scholar
  29. 29.
    Zhang YZ, Zhou B, Liu YX et al (2008) Fluorescence study on the interaction of bovine serum albumin with p-aminoazobenzene. J Fluoresc 1:109–118CrossRefGoogle Scholar
  30. 30.
    Zhang HM, Wang YQ, Zhou QH (2009) Investigation of the interactions of quercetin and morin with trypsin. Luminescence 5:355–362CrossRefGoogle Scholar
  31. 31.
    Hu YJ, Liu Y, Wang HB et al (2004) Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J Pharmaceut Biomed 4:915–919CrossRefGoogle Scholar
  32. 32.
    Gong AQ, Zhu XS, Hu YY et al (2007) A fluorescence spectroscopic study of the interaction between epristeride and bovin serum albumine and its analytical application. Talanta 4:668–673CrossRefGoogle Scholar
  33. 33.
    Soragni A, Zambelli B, Mukrasch MD et al (2008) Structural characterization of binding of Cu(II) to Tau protein. Biochemistry 41:10841–10851CrossRefGoogle Scholar
  34. 34.
    Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 11:3096–3102CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Bingjun Yang
    • 1
  • Rutao Liu
    • 1
  • Xiaopeng Hao
    • 2
  • Yongzhong Wu
    • 2
  • Jie Du
    • 2
  1. 1.Shandong Key Laboratory of Water Pollution Control and Resource ReuseSchool of Environmental Science and Engineering Shandong University, China–America CRC for Environment & HealthJinanPeople’s Republic of China
  2. 2.State Key Laboratory of Crystal MaterialsShandong UniversityJinanPeople’s Republic of China

Personalised recommendations