Molecular Interactions of Proteins and Peptides at Interfaces Studied by Sum Frequency Generation Vibrational Spectroscopy
- 15 December 2011
- journal article
- review article
- Published by American Chemical Society (ACS) in Langmuir
- Vol. 28 (4), 2113-2121
- https://doi.org/10.1021/la203823t
Abstract
Interfacial peptides and proteins are critical in many biological processes and thus are of interest to various research fields. To study these processes, surface sensitive techniques are required to completely describe different interfacial interactions intrinsic to many complicated processes. Sum frequency generation (SFG) spectroscopy has been developed into a powerful tool to investigate these interactions and mechanisms of a variety of interfacial peptides and proteins. It has been shown that SFG has intrinsic surface sensitivity and the ability to acquire conformation, orientation, and ordering information about these systems. This paper reviews recent studies on peptide/protein–substrate interactions, peptide/protein–membrane interactions, and protein complexes at interfaces and demonstrates the ability of SFG on unveiling the molecular pictures of complicated interfacial biological processes.Keywords
This publication has 92 references indexed in Scilit:
- Membrane Orientation of MSI-78 Measured by Sum Frequency Generation Vibrational SpectroscopyLangmuir, 2011
- Solvent Effect and Time-Dependent Behavior of C-Terminus-Cysteine-Modified Cecropin P1 Chemically Immobilized on a Polymer SurfaceLangmuir, 2011
- Investigating buried polymer interfaces using sum frequency generation vibrational spectroscopyProgress in Polymer Science, 2010
- Orientation Determination of Interfacial β-Sheet Structures in SituThe Journal of Physical Chemistry B, 2010
- Probing the Orientation of Surface-Immobilized Protein G B1 Using ToF-SIMS, Sum Frequency Generation, and NEXAFS SpectroscopyLangmuir, 2010
- Surface plasmon resonance for high‐throughput ligand screening of membrane‐bound proteinsBiotechnology Journal, 2009
- Probing the Orientation and Conformation of α-Helix and β-Strand Model Peptides on Self-Assembled Monolayers Using Sum Frequency Generation and NEXAFS SpectroscopyLangmuir, 2009
- Phospholipid flip-flop modulated by transmembrane peptides WALP and melittinJournal of Structural Biology, 2009
- In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopyJournal of Structural Biology, 2009
- Urea Orientation at Protein SurfacesJournal of the American Chemical Society, 2007