Surface Chemistry Influences Interfacial Fibrinogen Self-Association

Biomacromolecules
Blake B LangdonDaniel K Schwartz

Abstract

Surface chemistry modifications have been exploited in many applications in order to tune protein adsorption, layer formation, and aggregation. However, the kinetic processes by which surface chemistry influences protein adsorption and aggregation remain elusive. By combining intermolecular resonance energy transfer (RET) with high-throughput single-molecule tracking, we compared the dynamics of fibrinogen (Fg) interfacial self-associations on surfaces modified with hydrophobic trimethyl silane (TMS) or hydrophilic oligoethylene glycol (OEG). We directly observed interfacial, dynamic, and reversible Fg-Fg associations from low-RET (unassociated) to high-RET (associated) states. While isolated Fg molecule-TMS surface interactions were weaker than isolated Fg-OEG interactions, increasing protein concentration resulted in a more dramatic decrease in desorption from TMS than from OEG, such that at higher concentrations, Fg desorbed from TMS more slowly than from OEG. In addition to this observation, unassociated molecules were more likely to associate on TMS than on OEG, suggesting that the TMS surface promoted protein-protein associations. Importantly, increasing protein concentration also resulted in a greater increase in the len...Continue Reading

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Citations

Dec 15, 2015·ACS Applied Materials & Interfaces·Yu Cai, Daniel K Schwartz
May 30, 2017·ACS Applied Materials & Interfaces·Lydia KisleyDeborah E Leckband
Mar 1, 2018·Annual Review of Physical Chemistry·Nicholas A MoringoChristy F Landes
Sep 25, 2017·Langmuir : the ACS Journal of Surfaces and Colloids·Nicholas A MoringoChristy F Landes
Sep 17, 2020·Analytical Chemistry·William CalabraseLydia Kisley
Apr 27, 2018·Biomacromolecules·Lauren E JansenShelly R Peyton
Jul 10, 2019·Langmuir : the ACS Journal of Surfaces and Colloids·Evgeniy V DubrovinDmitry V Klinov

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