Abstract
PEGylation is the gold standard for constructing protein resistance surfaces. Herein, grafting mPEG-SH and SH-PEG-SH with varied molecular weights (Mw=5K, 10K, and 20K) on a gold chip, and the subsequent lysozyme adsorptions of the PEG layers are evaluated using quartz-crystal microbalance based on dissipation (QCM-D). The lysozyme resistance depends on the features of grafting density and chain conformation, i.e., linear and looped conformation. However, long-chain PEG (Mw≥10K) is insufficient to form a dense layer to resist protein due to large steric hindrances. Short-chain PEG (Mw=1K) with linear and looped structures is used to refill onto the long-chain PEG layer to increase the grafting density of PEGs and improve protein resistance. The refilling process and the subsequent protein adsorption depend on conformation rather than the density of the long-chain PEG substrate. Notably, the long-chain PEG looped substrates significantly improve protein resistance, attributing to the high viscoelasticity of the looped substrate and an increase in grafting density after refilling. Thus, refilling short-chain PEG improves protein resistance and the substrate conformation-dependence gives insight into the impact of topology, providing new ideas for how to increase chain density and select suitable topology to resist protein adsorption and demonstrating a potential application in biomedical fields.
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Brash, J. L.; Horbett, T. A.; Latour, R. A.; Tengvall, P. The blood compatibility challenge. Part 2: protein adsorption phenomena governing blood reactivity. Acta Biomater. 2019, 94, 11–24.
Bochenek, M.; Oleszko-Torbus, N.; Wałach, W.; Lipowska-Kur, D.; Dworak, A.; Utrata-Wesołek, A. Polyglycidol of linear or branched architecture immobilized on a solid support for biomedical applications. Polym. Rev. 2020, 60, 717–767.
Mevo, S. I. U.; Ashrafudoulla, M.; Furkanur Rahaman Mizan, M.; Park, S. H.; Ha, S. D. Promising strategies to control persistent enemies: some new technologies to combat biofilm in the food industry—a review. Compr. Rev. Food Sci. Food Saf. 2021, 20, 5938–5964.
Ye, Z.; Zhang, P.; Zhang, J.; Deng, L.; Zhang, J.; Lin, C.; Guo, R.; Dong, A. Novel dual-functional coating with underwater self-healing and anti-protein-fouling properties by combining two kinds of microcapsules and a zwitterionic copolymer. Prog. Org. Coat. 2019, 127, 211–221.
Sabaté del Río, J.; Henry, O. Y.; Jolly, P.; Ingber, D. E. An antifouling coating that enables affinity-based electrochemical biosensing in complex biological fluids. Nat. Nanotechnol. 2019, 14, 1143–1149.
Ahsan, S. M.; Rao, C. M.; Ahmad, M. Nanoparticle-protein interaction: the significance and role of protein corona. Mol. Cell. Toxicol. 2018, 175–198.
Hedayati, M.; Marruecos, D. F.; Krapf, D.; Kaar, J. L.; Kipper, M. J. Protein adsorption measurements on low fouling and ultralow fouling surfaces: a critical comparison of surface characterization techniques. Acta Biomater. 2020, 102, 169–180.
Cerchier, P.; Pezzato, L.; Gennari, C.; Moschin, E.; Moro, I.; Dabalà, M. PEO coating containing copper: A promising anticorrosive and antifouling coating for seawater application of AA 7075. Surf. Coat. Technol. 2020, 393, 125774.
Guo, L. L.; Cheng, Y. F.; Ren, X.; Gopinath, K.; Lu, Z. S.; Li, C. M.; Xu, L. Q. Simultaneous deposition of tannic acid and poly(ethylene glycol) to construct the antifouling polymeric coating on titanium surface. Colloids Surf. B: Biointerfaces 2021, 200, 111592.
Shin, E.; Lim, C.; Kang, U. J.; Kim, M.; Park, J.; Kim, D.; Choi, W.; Hong, J.; Baig, C.; Lee, D. W.; Kim, B. S. Mussel-inspired copolyether loop with superior antifouling behavior. Macromolecules 2020, 53, 3551–3562.
Aghajani, M.; Esmaeili, F. Anti-biofouling assembly strategies for protein & cell repellent surfaces: a mini-review. J. Biomater. Sci., Polym. Ed. 2021, 32, 1770–1789.
Zhang, K. X.; Huang, H.; Hung, H. C.; Leng, C.; Wei, S.; Crisci, R.; Jiang, S. Y.; Chen, Z. Strong hydration at the poly(ethylene glycol) brush/albumin solution interface. Langmuir 2020, 36, 2030–2036.
Hafeez, A.; Karim, Z. A.; Ismail, A. F.; Samavati, A.; Said, K. A. M.; Selambakkannu, S. Functionalized boron nitride composite ultrafiltration membrane for dye removal from aqueous solution. J. Membr. Sci. 2020, 612, 118473.
Wang, X.; Bowman, J.; Tu, S.; Nykypanchuk, D.; Kuksenok, O.; Minko, S. Polyethylene glycol Crowder’s effect on enzyme aggregation, thermal stability, and residual catalytic activity. Langmuir 2021, 37, 8474–8485.
Lu, J.; Xue, Y.; Shi, R.; Kang, J.; Zhao, C. Y.; Zhang, N. N.; Wang, C. Y.; Lu, Z. Y.; Liu, K. A non-sacrificial method for the quantification of poly(ethylene glycol) grafting density on gold nanoparticles for applications in nanomedicine. Chem. Sci. 2019, 10, 2067–2074.
Ortiz, R.; Olsen, S.; Thormann, E. Salt-induced control of the grafting density in poly(ethylene glycol) brush layers by a grafting-to approach. Langmuir 2018, 34, 4455–4464.
Wang, H.; Zhang, Z.; Chen, J.; Lian, C.; Han, X.; Liu, H. Conformation-dominated surface antifouling and aqueous lubrication. Colloids Surf. B: Biointerfaces 2022, 214, 112452.
Unsworth, L.; Sheardown, H.; Brash, J. Protein resistance of surfaces prepared by sorption of end-thiolated poly(ethylene glycol) to gold: effect of surface chain density. Langmuir 2005, 21, 1036–1041.
Unsworth, L. D.; Tun, Z.; Sheardown, H.; Brash, J. L. In situ neutron reflectometry investigation of gold-chemisorbed PEO layers of varying chain density: relationship of layer structure to protein resistance. J. Colloid Interface Sci. 2006, 296, 520–526.
Liu, Y. X.; Zhang, H. D. Structures and surface states of polymer brushes in good solvents: effects of surface interactions. Chinese J. Polym. Sci. 2018, 36, 1047–1054.
Penna, M.; Ley, K. J.; Belessiotis-Richards, A.; MacLaughlin, S.; Winkler, D. A.; Yarovsky, I. Hydration and dynamics of ligands determine the antifouling capacity of functionalized surfaces. J. Phys. Chem. C 2019, 123, 30360–30372.
Jeon, S.; Lee, J.; Andrade, J.; De Gennes, P. Protein—surface interactions in the presence of polyethylene oxide: I. Simplified theory. J. Colloid Interface Sci. 1991, 142, 149–158.
Benhabbour, S. R.; Sheardown, H.; Adronov, A. Protein resistance of PEG-functionalized dendronized surfaces: effect of PEG molecular weight and dendron generation. Macromolecules 2008, 41, 4817–4823.
Chen, Q.; Yu, S.; Zhang, D.; Zhang, W.; Zhang, H.; Zou, J.; Mao, Z.; Yuan, Y.; Gao, C.; Liu, R. Impact of antifouling PEG layer on the performance of functional peptides in regulating cell behaviors. J. Am. Chem. Soc. 2019, 141, 16772–16780.
Wang, H.; Dardir, K.; Lee, K. B.; Fabris, L. Impact of protein corona in nanoflare-based biomolecular detection and quantification. Bioconjugate Chem. 2019, 30, 2555–2562.
Dai, Q.; Walkey, C.; Chan, W. C. Polyethylene glycol backfilling mitigates the negative impact of the protein corona on nanoparticle cell targeting. Angew. Chem. Int. Ed. 2014, 53, 5093–5096.
Du, Y.; Jin, J.; Jiang, W. A study of polyethylene glycol backfilling for enhancing target recognition using QCM-D and DPI. J. Mater. Chem. B 2018, 6, 6217–6224.
Hu, Y.; Jin, J.; Han, Y.; Yin, J.; Jiang, W.; Liang, H. Study of fibrinogen adsorption on poly(ethylene glycol)-modified surfaces using a quartz crystal microbalance with dissipation and a dual polarization interferometry. RSC Adv. 2014, 4, 7716–7724.
Jin, J.; Han, Y.; Zhang, C.; Liu, J.; Jiang, W.; Yin, J.; Liang, H. Effect of grafted PEG chain conformation on albumin and lysozyme adsorption: a combined study using QCM-D and DPI. Colloids Surf., B 2015, 136, 838–844.
Li, B.; Yu, B.; Wang, X. L.; Guo, F.; Zhou, F. Correlation between conformation change of polyelectrolyte brushes and lubrication. Chinese J. Polym. Sci. 2015, 33, 163–172.
Han, Y.; Ma, J.; Hu, Y.; Jin, J.; Jiang, W. Effect of end-grafted polymer conformation on protein resistance. Langmuir 2018, 34, 2073–2080.
Du, Y.; Jin, J.; Liang, H.; Jiang, W. Structural and physicochemical properties and biocompatibility of linear and looped polymer-capped gold nanoparticles. Langmuir 2019, 35, 8316–8324.
Lv, J.; Jin, J.; Han, Y.; Jiang, W. Effect of end-grafted PEG conformation on the hemocompatibility of poly(styrene-b-(ethylene-co-butylene)-b-styrene). J. Biomater. Sci., Polym. Ed. 2019, 30, 1670–1685.
Alexander, S. Adsorption of chain molecules with a polar head a scaling description. J. Phys. I 1977, 38, 983–987.
Jin, J.; Hu, Y.; Han, Y.; Jiang, W. Modified surface by poly(ethylene glycol) with looped conformation and its superior anticoagulant property. Sci. Sin. Chim. 2018, 48, 972–980.
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This work was financially supported by the National Natural Science Foundation of China (No. 52073276), Changchun Science and Technology Development Program (No. 21ZY07), and the Innovation and Entrepreneurship Talent Project of Jilin Province.
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Li, C., Zhang, JN., Jin, J. et al. The Effect of Topologies and Refilling Short-chain PEG on Protein Adsorption. Chin J Polym Sci 41, 1879–1888 (2023). https://doi.org/10.1007/s10118-023-2971-x
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DOI: https://doi.org/10.1007/s10118-023-2971-x