Lipid-like behavior of signal sequence peptides at air?water interface

AMBROGGIO E.E.,; FIDELIO G.D.

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2013 vol. 1828 p. 708 - 708

a b s t r a c tSeveral protein transport processes in the cell are mediated by signal sequence peptides located at the N-terminal side of the mature protein sequence. To date, the specific interaction and the stability of these peptides at the amphipathic interface of biological membranes and the relevance of the peptide conformation when they interact with lipids is not clear. We report the surface properties and the peptide?lipid interaction of three signal sequence peptides at the air?NaCl 145 mM interface by using the Langmuir monolayer approach. These synthetic peptides have a natural sequence with a non-periodic amphiphilicity, where hydrophobic and hydrophilic residues are located on opposed sides of the peptide primary sequence. We show that signal sequence peptides form insoluble monolayers of high stability against lateral compression. At closepacking, peptide molecular area, surface potential and the high stability of the peptide monolayer are indicative