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

The solid-phase synthesis of a novel amphiphilic peptide conjugate I, contg. in the same mol. three different functions: N,N-bis[2-[bis(carboxyethyl)amino]ethyl]-L-glutamic acid chelating agent, the CCK8 bioactive peptide, and a hydrophobic moiety contg. four alkyl chains with 18 carbon atoms each, is reported. In water soln. at pH 7.4, I self-assembles in very stable micelles at very low concn. [crit. micellar concn. (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 no. of 39  2 and the two micellar axes of about 52 and 26 .