Asp-Gly based peptides confined at the surface of cationic gemini surfactant aggregates.
Cationic gemini surfactants complexed with anionic oligoglycine-aspartate (called gemini peptides hereafter) were synthesized, and their aggregation behaviors were studied. The effects of the hydrophobic chain length (C10-C22) and the length of the oligoglycine (0-4) were investigated, and it was clearly shown by critical micellar concentration, Krafft temperature, and isothermal surface pressure measurements that the hydrophobic effect and interpeptidic interaction influence the aggregation behavior in a cooperative manner. Below their Krafft temperatures, some of them formed both hydro- and organogels with three-dimensional networks and the Fourier transform infrared measurements show the presence of interpeptidic hydrogen bonds.
Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, 33607 Pessac Cedex, France.
Aurélie
A
Brizard
Christel
C
Dolain
Ivan
I
Huc
Reiko
R
Oda
D001224:Aspartic Acid / Q000737:chemistry*; D002412:Cations / Q000737:chemistry*; D004553:Electric Conductivity; D006860:Hydrogen Bonding; D008823:Micelles; D008956:Models, Chemical; D009842:Oligopeptides / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011312:Pressure; D012542:Scattering, Radiation; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties; D013501:Surface-Active Agents / Q000737:chemistry*; D013696:Temperature; D014965:X-Rays
D002412:Cations; D008823:Micelles; D009842:Oligopeptides; D010455:Peptides; D013501:Surface-Active Agents; D001224:Aspartic Acid