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Synthesis and conformational characterization in the solid state of peptides consisting of L ‐phenylalanyl‐ L ‐phenylalanylglycyl and L ‐phenylalanyl‐ L ‐leucylglycyl residues
Author(s) -
Katakai Ryoichi,
Nakayama Yoko
Publication year - 1981
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1981.360201004
Subject(s) - chemistry , tripeptide , peptide , stereochemistry , solid state , helix (gastropod) , biochemistry , ecology , snail , biology
Two series of peptides containing L ‐phenylalanine, Nps‐( L ‐Phe‐ L ‐Phe‐Gly) n ‐OEt ( n = 1–6) and Nps‐( L ‐Phe‐ L ‐Leu‐Gly) n ‐OEt ( n = 1–7), were prepared by the fragment‐condensation method using the tripeptide N ‐hydroxysuccinimide esters. Conformational characterization of these peptides in the solid state was performed by ir spectroscopy and x‐ray powder diffraction measurement. The peptides Nps‐( L ‐Phe‐ L ‐Phe‐Gly) n ‐OEt take the β‐structure, but the pentadecapeptide and higher peptides of Nps‐( L ‐Phe‐ L ‐Leu‐Gly) n ‐OEt form the α‐helix, although the lower homologs take the β‐structure.