N- and Calpha-methylation in biologically active peptides: synthesis, structural and functional aspects.
Numerous backbone constraints can be used to develop pseudopeptides or pseudomimetics of biologically active peptides. Among those, N- and Calpha-methyl amino acids that can be incorporated by solid-phase peptide synthesis in a bioactive sequence represent important tools to restrict phi and psi angles of peptide backbone. This review will focus on the chemical syntheses of N- and Calpha-methyl amino acids, their effects on peptide conformation and structure, and their role on the peptide stability towards enzymatic degradation and on the biological activities of the resulting analogues.
Sagan
Sandrine
S
UMR 7613 CNRS-Université Pierre & Marie Curie, Structure and Function of Bioactive Molecules, Case courrier 182, 4 place Jussieu, 75005 Paris, France. sagan@ccr.jussieu.fr
Karoyan
Philippe
P
Lequin
Olivier
O
Chassaing
Gérard
G
Lavielle
Solange
S
D000596:Amino Acids / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D006801:Humans; D008745:Methylation; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*
D000596:Amino Acids; D010455:Peptides