Document Detail

Orientation determination of interfacial beta-sheet structures in situ.
MedLine Citation:
PMID:  20504035     Owner:  NLM     Status:  MEDLINE    
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 alpha-helical and beta-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 beta-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 beta-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 (theta) and the twist angle (psi) of the beta-sheet at interfaces are determined. The developed method in this paper can be used to obtain in situ structural information of beta-sheet components in complex molecules. The combination of this method and the existing methodology that is currently used to investigate alpha-helical structures will greatly broaden the application of optical spectroscopy in physical chemistry, biochemistry, biophysics, and structural biology.
Khoi Tan Nguyen; John Thomas King; Zhan Chen
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  The journal of physical chemistry. B     Volume:  114     ISSN:  1520-5207     ISO Abbreviation:  J Phys Chem B     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-06-24     Completed Date:  2010-09-22     Revised Date:  2014-09-17    
Medline Journal Info:
Nlm Unique ID:  101157530     Medline TA:  J Phys Chem B     Country:  United States    
Other Details:
Languages:  eng     Pagination:  8291-300     Citation Subset:  IM    
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MeSH Terms
Amino Acid Sequence
Anti-Infective Agents / chemistry*
Antimicrobial Cationic Peptides / chemistry*
DNA-Binding Proteins / chemistry*
Lipid Bilayers / chemistry,  metabolism
Molecular Sequence Data
Peptides, Cyclic / chemistry*
Polymers / chemistry
Protein Structure, Secondary
Spectroscopy, Fourier Transform Infrared
Spectrum Analysis, Raman
Grant Support
1R01GM081655-01A2/GM/NIGMS NIH HHS; R01 GM081655/GM/NIGMS NIH HHS; R01 GM081655-01A2/GM/NIGMS NIH HHS
Reg. No./Substance:
0/Anti-Infective Agents; 0/Antimicrobial Cationic Peptides; 0/DNA-Binding Proteins; 0/Lipid Bilayers; 0/Peptides, Cyclic; 0/Polymers; 118231-04-2/tachyplesin peptide, Tachypleus tridentatus

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