Interfacial orientation and secondary structure change in tachyplesin I: Molecular dynamics and sum frequency generation spectroscopy studies

Boughton, Andrew P., Nguyen, Khoi, Andricioaei, Ioan and Chen, Zhan (2011) Interfacial orientation and secondary structure change in tachyplesin I: Molecular dynamics and sum frequency generation spectroscopy studies. Langmuir, 27 23: 14343-14351. doi:10.1021/la203192c


Author Boughton, Andrew P.
Nguyen, Khoi
Andricioaei, Ioan
Chen, Zhan
Title Interfacial orientation and secondary structure change in tachyplesin I: Molecular dynamics and sum frequency generation spectroscopy studies
Journal name Langmuir   Check publisher's open access policy
ISSN 0743-7463
1520-5827
Publication date 2011-12-06
Year available 2011
Sub-type Article (original research)
DOI 10.1021/la203192c
Open Access Status
Volume 27
Issue 23
Start page 14343
End page 14351
Total pages 9
Place of publication Washington, DC United States
Publisher American Chemical Society
Collection year 2012
Language eng
Subject 1603 Demography
3104 Condensed Matter Physics
3110 Surfaces and Interfaces
2500 Materials Science
1607 Social Work
Abstract Recent advances in the collection and interpretation of surface-sensitive vibrational spectroscopic measurements have made it possible to study the orientation of peptides and proteins in situ in a biologically relevant environment. However, interpretation of sum frequency generation (SFG) and attenuated total reflectance Fourier transform infrared (ATR-FTIR) vibrational spectroscopy is hindered by the fact that orientation cannot be inferred without some prior knowledge of the protein structure. In this work, molecular dynamics simulations were used to study the interfacial orientation and structural deformation of the short β-sheet peptide tachyplesin I at the polystyrene/water interface. By combining these results with ATR-FTIR and SFG measurements, reasonable agreement was found with the simulation results, suggesting that tachyplesin I lies parallel to the surface, although the simulation results imply a broader distribution of peptide twist angles than could be characterized using available experimental measurements. The interfacial structure was found to be deformable even when disulfide bonds were preserved, and these local deviations from a purely extended β-sheet conformation may be of importance to future developments in the interpretation of SFG and ATR-FTIR spectra.
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
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 12 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 13 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Wed, 06 Aug 2014, 16:17:33 EST by System User on behalf of School of Chemical Engineering