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  • Title: Micelles by self-assembling peptide-conjugate amphiphile: synthesis and structural characterization.
    Author: Accardo A, Tesauro D, Del Pozzo L, Mangiapia G, Paduano L, Morelli G.
    Journal: J Pept Sci; 2008 Aug; 14(8):903-10. PubMed ID: 18320561.
    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 x 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 A.
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