Premium
Pilin C‐terminal peptide binds asialo‐GM 1 in liposomes: A 2 H‐NMR study
Author(s) -
Jones David H.,
Barber Kathryn R.,
Grant Chris W. M.,
Hodges Robert S.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560061120
Subject(s) - peptide , pilin , chemistry , liposome , stereochemistry , receptor , biochemistry , glycosphingolipid , nuclear magnetic resonance spectroscopy , biophysics , moiety , biology , pilus , escherichia coli , gene
Wideline 2 H‐NMR observations are described demonstrating the interaction of a synthetic peptide (PAK), representing residues 128‐144 of the binding domain of pilin surface protein from Pseudomonas aeruginosa , with a complex glycosphingolipid thought to be its natural receptor. The receptor glycolipid (asialo‐GM 1 ) carried 2 H probe nuclei on the terminal and next‐to‐terminal carbohydrate residues and was present as a minor component in fluid phosphatidylcholine liposomes. The peptide induced spectral changes that could be understood as arising from receptor motional changes, without receptor immobilization on the NMR time scale of 10 4 s −1 . Spectral effects were reversed by reduction of the single peptide disulfide bond—a structural feature previously shown to be a determinant of PAK conformation (Campbell AP, McInnes C, Hodges RS, Sykes BD. 1995. Biochemistry 34:6255‐16268). This is the first demonstration of PAK interaction with its epithelial cell receptor in liposomes.