The Journal of Membrane Biology

, Volume 249, Issue 3, pp 411–417 | Cite as

In Situ Investigation of Peptide–Lipid Interaction Between PAP248–286 and Model Cell Membranes

  • Khoi Tan NguyenEmail author


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.


Gel-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.

Supplementary material

232_2016_9878_MOESM1_ESM.docx (34 kb)
Supplementary material 1 (DOCX 34 kb)


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Copyright information

© Springer Science+Business Media New York 2016

Authors and Affiliations

  1. 1.School of Chemical EngineeringThe University of QueenslandBrisbaneAustralia
  2. 2.School of BiotechnologyInternational University, Vietnam National University Ho Chi Minh CityVietnam

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