A new molecular scaffold for the formation of supramolecular peptide double helices: the crystallographic insight.
[structure: see text]. A series of water-soluble synthetic dipeptides (1-3) with an N-terminally located beta-alanine residue, beta-alanyl-l-valine (1), beta-alanyl-l-isoleucine (2), and beta-alanyl-l-phenylalanine (3), form hydrogen-bonded supramolecular double helices with a pitch length of 1 nm, whereas the C-terminally positioned beta-alanine containing dipeptide (4), l-phenylalanyl-beta-alanine, does not form a supramolecular double helical structure. beta-Ala-Xaa (Xaa = Val/Ile/Phe) can be regarded as a new motif for the formation of supramolecular double helical structures in the solid state.
Guha
Samit
S
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.
Drew
Michael G B
MG
Banerjee
Arindam
A
D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000138:chemical synthesis* / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary
D004151:Dipeptides