3338-40-7Relevant articles and documents
Macrocyclization of Peptide Side Chains by the Ugi Reaction: Achieving Peptide Folding and Exocyclic N-Functionalization in One Shot
Vasco, Aldrin V.,Pérez, Carlos S.,Morales, Fidel E.,Garay, Hilda E.,Vasilev, Dimitar,Gavín, José A.,Wessjohann, Ludger A.,Rivera, Daniel G.
, p. 6697 - 6707 (2015/10/06)
The cyclization of peptide side chains has been traditionally used to either induce or stabilize secondary structures (β-strands, helices, reverse turns) in short peptide sequences. So far, classic peptide coupling, nucleophilic substitution, olefin metat
Intramolecular ligation of carbonyl oxygen to central zinc in synthetic oligopeptide-linked zinc-porphyrins
Tamiaki,Kiyomori,Maruyama
, p. 2478 - 2486 (2007/10/02)
Oligopeptide-linked zinc-porphyrins were prepared (oligopeptide = -Phe(m)-Ala(n)-OMe and porphyrin = 5,15-diaryl-2,3,7,8,12,13,17,18-octaethylporphyrin). 1H NMR, IR, visible, and CD spectra of the synthetic molecule in a chlorinated methane (CDCl3 or CH2Cl2) showed that the carbonyl oxygen of the N-terminal amino acid of the linked peptide should ligate the central zine metal in the molecule as the axial ligand to form a pentacoordinated zinc-porphyrin. The coordination of the zinc with the peptide framework changed the optical and electrical properties, indicating that such ligation might control the reactivity in biological metallotetrapyrrole-protein systems as well as the coordination to the peptide residue.