L
Lingyan Li
Researcher at University of Akron
Publications - 31
Citations - 5557
Lingyan Li is an academic researcher from University of Akron. The author has contributed to research in topics: Protein adsorption & Adsorption. The author has an hindex of 28, co-authored 31 publications receiving 5031 citations. Previous affiliations of Lingyan Li include Cleveland Clinic & Kansas State University.
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Journal ArticleDOI
Surface Hydration: Principles and Applications Toward Low-fouling/nonfouling Biomaterials
TL;DR: In this article, two major classes of non-fouling materials (i.e., hydrophilic and zwitterionic materials) and associated basic non fouling mechanisms and practical examples are discussed.
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Strong resistance of phosphorylcholine self-assembled monolayers to protein adsorption: insights into nonfouling properties of zwitterionic materials.
TL;DR: The strong resistance of zwitterionic phosphorylcholine (PC) self-assembled monolayers (SAMs) to protein adsorption is shown and key factors leading to their nonfouling behavior are examined using both experimental and molecular simulation techniques.
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Protein adsorption on oligo(ethylene glycol)-terminated alkanethiolate self-assembled monolayers: The molecular basis for nonfouling behavior.
TL;DR: For EG2OH- and EG4OH- SAMs, proteins adsorb more on the densely packed SAMs prepared from mixed ethanol and water solutions, while EG6OH-SAMs generally resist protein adsorption regardless of the assembly solvent used.
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Strong Repulsive Forces between Protein and Oligo (Ethylene Glycol) Self-Assembled Monolayers: A Molecular Simulation Study
TL;DR: Results show that a tightly bound water layer adjacent to the OEG-SAMs is mainly responsible for the large repulsive hydration force.
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Molecular simulation study of water interactions with oligo (ethylene glycol)-terminated alkanethiol self-assembled monolayers.
TL;DR: It appears that there is a correlation between OEG surface resistance to protein adsorption and the surface density of OEG chains, which leads to a large number of tightly bound water molecules around O EG chains and the rapid mobility of hydrated SAM chains.