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Unexpectedly Resisting Protein Adsorption on Self-assembled Monolayers Terminated with Two Hydrophilic Hydroxyl Groups by Mao, Dangxin; Wu, Yuan-Yan; Tu, Yusong is a scholarly article available to read on EtoBox.

What is Unexpectedly Resisting Protein Adsorption on Self-assembled Monolayers Terminated with Two Hydrophilic Hydroxyl Groups about?

The OH-terminated self-assembled monolayers, as protein-resistant surfaces, have significant potential in biocompatible implant devices, which can avoid or reduce adverse reactions caused by protein adhesion to biomaterial surfaces, such as thrombosis, immune response and inflammation. Here, molecular dynamics simulations were performed to evaluate the degree of protein adsorption on the self-assembled monolayer terminated with two hydrophilic OH groups ((OH)2-SAM) at the packing densities ({\Sigma}) of 4.5 nm-2 and 6.5 nm-2, respectively. The results show that the (OH)2-SAM itself can significantly improve the performance of its resistance to protein adsorption. This is attributed to the structure of the (OH)2-SAM itself, i.e., the formation of a nearly perfect hexagonal-ice-like hydrogen bond structure in the OH matrix of the (OH)2-SAM at {\Sigma} = 4.5 nm-2, which sharply reduces the number of hydrogen bonds (i.e., 0.9) formed between the hydrophobic (OH)2-SAM surface and protein. While for {\Sigma} = 6.5 nm-2, the hydrophilic (OH)2-SAM surface can provide more hydrogen bonding sites to form hydrogen bonds (i.e., 7.3) with protein. The number of hydrogen bonds formed between the

Author

Mao, Dangxin; Wu, Yuan-Yan; Tu, Yusong

Published

2022

Language

EN