In Situ Investigation of Peptide–Lipid Interaction Between PAP248–286 and Model Cell Membranes
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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.
KeywordsGel-phase and fluid-phase model lipid bilayers PAP248–286 Peptide conformation SDS micelles
This research is funded by the Vietnam National Foundation for Science and Technology Development (NAFOSTED) under Grant Number 106.16-2012.67. The author sincerely thanks Dr. Gay Marsden for her generous assistance in the manuscript preparation.
Compliance with Ethical Standards
Conflict of interest
The authors declare no competing financial interests.
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