Detection of amide I signals of interfacial proteins in situ using SFG.
In this Communication, we demonstrate the novel observation that it is feasible to collect amide signals from polymer/protein solution interfaces in situ using sum frequency generation (SFG) vibrational spectroscopy. Such SFG amide signals allow for acquisition of more detailed molecular level information of entire interfacial protein structures. Proteins investigated include bovine serum albumin, mussel protein mefp-2, factor XIIa, and ubiquitin. Our studies indicate that different proteins generate different SFG amide signals at the polystyrene/protein solution interface, showing that they have different interfacial coverage, secondary structure, or orientation.
Wang
Jie
J
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Even
Mark A
MA
Chen
Xiaoyun
X
Schmaier
Alvin H
AH
Waite
J Herbert
JH
Chen
Zhan
Z
D000042:Absorption; D000577:Amides / Q000032:analysis / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D057927:Hydrophobic and Hydrophilic Interactions; D011108:Polymers / Q000737:chemistry; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013057:Spectrum Analysis / Q000379:methods*; D013499:Surface Properties; D025801:Ubiquitin / Q000737:chemistry*
D000577:Amides; D011108:Polymers; D025801:Ubiquitin; D012710:Serum Albumin, Bovine