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Elucidating Changes in Interfacial Water Structure upon Protein Adsorption
Author(s) -
Kim Joonyeong,
Cremer Paul S.
Publication year - 2001
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/1439-7641(20010917)2:8/9<543::aid-cphc543>3.0.co;2-5
Subject(s) - adsorption , chemistry , hydrogen bond , molecule , bovine serum albumin , sum frequency generation , spectroscopy , protein adsorption , infrared spectroscopy , analytical chemistry (journal) , crystallography , chromatography , organic chemistry , nonlinear optics , physics , nonlinear system , quantum mechanics
A coat to fit the body: Although protein adsorption onto surfaces is a complicated process, sum‐frequency generation (SFG) spectroscopy probes the interfacial water structure around a silica surface as a model protein (bovine serum albumin, BSA) adsorbs onto it from solution. At pH 8.0, the attenuated SFG intensity after BSA adsorption indicates that interfacial water molecules are less ordered due to a reduction in surface ξ ‐potential. The SFG spectrum shows the C−O stretching vibrations subject to stronger ( $\tilde \vartheta$ ≈3200 cm −1 ) and weaker (3200 cm −1 ) hydrogen bonds