Orientation determination of interfacial β-sheet structures in situ

Nguyen, Khoi Tan, King, John Thomas and Chen, Zhan (2010) Orientation determination of interfacial β-sheet structures in situ. Journal of Physical Chemistry B, 114 25: 8291-8300. doi:10.1021/jp102343h

Author Nguyen, Khoi Tan
King, John Thomas
Chen, Zhan
Title Orientation determination of interfacial β-sheet structures in situ
Journal name Journal of Physical Chemistry B   Check publisher's open access policy
ISSN 1520-6106
Publication date 2010-07-01
Year available 2010
Sub-type Article (original research)
DOI 10.1021/jp102343h
Open Access Status
Volume 114
Issue 25
Start page 8291
End page 8300
Total pages 10
Place of publication Washington, DC United States
Publisher American Chemical Society
Collection year 2011
Language eng
Subject 1606 Political Science
2505 Materials Chemistry
2508 Surfaces, Coatings and Films
Abstract Structural information such as orientations of interfacial proteins and peptides is important for understanding properties and functions of such biological molecules, which play crucial roles in biological applications and processes such as antimicrobial selectivity, membrane protein activity, biocompatibility, and biosensing performance. The α-helical and β-sheet structures are the most widely encountered secondary structures in peptides and proteins. In this paper, for the first time, a method to quantify the orientation of the interfacial β-sheet structure using a combined attenuated total reflectance Fourier transformation infrared spectroscopic (ATR-FTIR) and sum frequency generation (SFG) vibrational spectroscopic study was developed. As an illustration of the methodology, the orientation of tachyplesin I, a 17 amino acid peptide with an antiparallel β-sheet, adsorbed to polymer surfaces as well as associated with a lipid bilayer was determined using the regular and chiral SFG spectra, together with polarized ATR-FTIR amide I signals. Both the tilt angle (θ) and the twist angle (Ψ) of the β-sheet at interfaces are determined. The developed method in this paper can be used to obtain in situ structural information of β-sheet components in complex molecules. The combination of this method and the existing methodology that is currently used to investigate α-helical structures will greatly broaden the application of optical spectroscopy in physical chemistry, biochemistry, biophysics, and structural biology.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemical Engineering Publications
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