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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

✍ Scribed by Ryoichi Katakai; Yoko Nakayama


Publisher
Wiley (John Wiley & Sons)
Year
1981
Tongue
English
Weight
435 KB
Volume
20
Category
Article
ISSN
0006-3525

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✦ Synopsis


Abstract

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.


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