Anionic phospholipids can mediate membrane insertion of the anionic part of a bound peptide.
The effect of anionic lipids on the membrane insertion of a carboxyl group on a specially designed palmitoylated peptide was studied, using tryptophan fluorescence. It is demonstrated that the negatively charged membrane surface of mixed phosphatidylcholine/phosphatidylglycerol small unilamellar vesicles enhances the protonation of the C-terminal carboxyl group, and the subsequent insertion of that part of the peptide.
Leenhouts
J M
JM
Department of Biochemistry of Membranes (CBLE), Utrecht University, The Netherlands.
van den Wijngaard
P W
PW
de Kroon
A I
AI
de Kruijff
B
B
D000595:Amino Acid Sequence; D000838:Anions / Q000737:chemistry*; D001120:Arginine; D002021:Buffers; D006863:Hydrogen-Ion Concentration; D008051:Lipid Bilayers / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D011522:Protons; D013050:Spectrometry, Fluorescence; D013499:Surface Properties; D014364:Tryptophan
D000838:Anions; D002021:Buffers; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010455:Peptides; D010743:Phospholipids; D011522:Protons; D014364:Tryptophan; D001120:Arginine