Micelles by self-assembling peptide-conjugate amphiphile: synthesis and structural characterization

✍ Scribed by Antonella Accardo; Diego Tesauro; Luigi Del Pozzo; Gaetano Mangiapia; Luigi Paduano; Giancarlo Morelli

• Publisher: John Wiley and Sons
• Year: 2008
• Tongue: English
• Weight: 289 KB
• Volume: 14
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.1024

✦ Synopsis

Abstract

The chemical synthesis by solid‐phase methods of a novel amphiphilic peptide, peptide‐conjugate amphiphile (PCA), containing in the same molecule three different functions: (i) the N,N‐bis[2‐[bis(carboxy‐ethyl)amino]ethyl]‐L‐glutamic acid (DTPAGlu) chelating agent, (ii) the CCK8 bioactive peptide, and (iii) a hydrophobic moiety containing four alkyl chains with 18 carbon atoms each, is reported. In water solution at pH 7.4, PCA self‐assembles in very stable micelles at very low concentration [critical micellar concentration (cmc) values of 5 × 10^−7^ mol kg^−1^] as confirmed by fluorescence spectroscopy. The structural characterization, obtained with small‐angle neutron scattering (SANS) measurements, indicates that the aggregates are substantially represented by ellipsoidal micelles with an aggregation number of 39 ± 2 and the two micellar axes of about 52 and 26 Å. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.