Premium
X‐ray reflectivity study of a transcription‐activating factor‐derived peptide penetration into the model phospholipid monolayers
Author(s) -
Tae Giyoong,
Yang Hosung,
Shin Kwanwoo,
Satija Sushil K.,
Torikai Naoya
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.948
Subject(s) - monolayer , penetration (warfare) , chemistry , peptide , phospholipid , bilayer , surface pressure , membrane , adsorption , lipid bilayer , x ray reflectivity , biophysics , biochemistry , organic chemistry , nanotechnology , materials science , physics , mechanics , engineering , biology , thin film , operations research
The penetration of a transcription‐activating factor (TAT)‐derived, cell‐penetration peptide onto 1,2‐dipalmitoyl‐ sn ‐glycero‐3‐phosphocholine (DPPC) or 1,2‐dipalmitoyl‐ sn ‐glycero‐3‐[phospho‐ L ‐serine] (DPPS) monolayer on phosphate‐buffered saline subphase was characterized. The surface area at the target pressure increased noticeably by the peptide penetration from the subphase to the phospholipid monolayer, which might suggest a direct penetration of the peptide across the pure phospholipid bilayer membrane. Interestingly, the more significant area increase at 35 mN/m was monitored from DPPC monolayer, contrary to the simple charge interaction: the net neutral DPPC, the net‐negative DPPS, and the positive TAT‐derived peptides (TDP). X‐ray reflectivity measurements as well as the molecular area from π (surface pressure)‐ A (area) isotherms suggest that the packing density of DPPS at the target pressure is too high to allow the effective penetration of the peptide into the monolayer and the positively charged peptides can be entrapped at the negative electrostatic well of DPPS headgroup layer, leading to the simple adsorption on the DPPS monolayer instead of penetration into it. Thus, more penetration with less adsorption of the peptide is induced by DPPC monolayer than DPPS monolayer. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.