In situ investigation of peptide–lipid interaction between PAP248–286 and model cell membranes

Nguyen, Khoi Tan (2016) In situ investigation of peptide–lipid interaction between PAP248–286 and model cell membranes. Journal of Membrane Biology, 249 3: 411-417. doi:10.1007/s00232-016-9878-1


Author Nguyen, Khoi Tan
Title In situ investigation of peptide–lipid interaction between PAP248–286 and model cell membranes
Formatted title
In situ investigation of peptide–lipid interaction between PAP248–286 and model cell membranes
Journal name Journal of Membrane Biology   Check publisher's open access policy
ISSN 1432-1424
0022-2631
Publication date 2016-02-16
Year available 2016
Sub-type Article (original research)
DOI 10.1007/s00232-016-9878-1
Open Access Status Not Open Access
Volume 249
Issue 3
Start page 411
End page 417
Total pages 7
Place of publication New York, NY, United States
Publisher Springer New York LLC
Language eng
Formatted abstract
Sum frequency generation vibrational spectroscopy (SFG) was utilized to investigate the interaction between PAP248–286 and the two lipid bilayer systems. The present study also provides spectroscopic evidence to confirm that, although PAP248–286 is unable to penetrate into the hydrophobic core of the lipid bilayers, it is capable of interacting more intimately with the fluid-phase POPG/POPC than with the gel-phase DPPG/DPPC lipid bilayer. The helical structure content of lipid-bound PAP248–286 was also observed to be high, in contrast to the results previously reported using nuclear magnetic resonance (NMR). Collectively, our SFG data suggest that lipid-bound PAP248–286 actually resembles its structure in 50 % 2,2,2-trifluoroethanol better than the structure when the peptide binds to SDS micelles. This present study questions the use of SDS micelles as the model membrane for NMR studies of PAP248–286 due to its protein denaturing activity.
Keyword Gel-phase model lipid bilayers
Fluid-phase model lipid bilayers
PAP248–286
Peptide conformation
SDS micelles
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

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