Solid-phase synthesis and characterization of a novel fullerene-peptide derived from histone H3.
A peptide analogue from a histone H3 protein containing the L-fulleropyrrolidino-glutamic acid has been prepared by a solid-phase approach and has been fully characterized. By molecular modelling it was verified that this peptide derivative is able to retain a binding capacity to the MHC (major histocompatibility complex) molecule similar to that of the cognate epitope.
Bianco
Alberto
A
Institute of Molecular and Cellular Biology, UPR 9021 CNRS, 67084 Strasbourg, France. A.Bianco@ibmc.u-strasbg.fr
Pantarotto
Davide
D
Hoebeke
Johan
J
Briand
Jean-Paul
JP
Prato
Maurizio
M
D002851:Chromatography, High Pressure Liquid; D000939:Epitopes / Q000737:chemistry / Q000276:immunology; D037741:Fullerenes / Q000737:chemistry*; D018698:Glutamic Acid / Q000737:chemistry; D006657:Histones / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000276:immunology; D017434:Protein Structure, Tertiary
D000939:Epitopes; D037741:Fullerenes; D006657:Histones; D010455:Peptides; D018698:Glutamic Acid