102029-85-6Relevant articles and documents
A new molecular scaffold for the formation of supramolecular peptide double helices: The crystallographic insight
Guha, Samit,Drew, Michael G. B.,Banerjee, Arindam
, p. 1347 - 1350 (2007/12/29)
A series of water-soluble synthetic dipeptides (1-3) with an N-terminally located β-alanine residue, β-alanyl-L-valine (1), β-alanyl-L- isoleucine (2), and β-alanyl-L-phenylalanine (3), form hydrogen-bonded supramolecular double helices with a pitch length of 1 nm, whereas the C-terminally positioned β-alanine containing dipeptide (4), L-phenylalanyl-β-alanine, does not form a supramolecular double helical structure. β-Ala-Xaa (Xaa = Val/lle/Phe) can be regarded as a new motif for the formation of supramolecular double helical structures in the solid state.