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Solid-state conformation of copolymers of β-benzyl-L-aspartate with L-alanine, L-leucine, L-valine, γ-benzyl-L-glutamate, or ϵ-carbobenzoxy-L-lysine

✍ Scribed by Willem L. Sederel; Adriaan Bantjes; Jan Feijen; James M. Anderson

Publisher
Wiley (John Wiley & Sons)
Year
1980
Tongue
English
Weight
608 KB
Volume
19
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The solid‐state conformation of copolymers of β‐benzyl‐L‐aspartate [L‐Asp(OBzl)] with L‐leucine (L‐Leu), L‐alanine (L‐Ala), L‐valine (L‐Val), γ‐benzyl‐L‐glutamate [L‐Glu(OBzl)], or ϵ‐carbobenzoxy‐L‐lysine (Cbz‐L‐Lys) has been studied by ir spectroscopy and circular dichroism (CD). The ir spectra in the region of the amide I and II bands and in the region of 700–250 cm^−1^ have been determined. The results from the ir studies are in good agreement with data obtained by CD experiments. Incorporation of the amino acid residues mentioned above into poly[L‐Asp(OBzl)] induces a change from the left‐handed into the right‐handed α‐helix. This conformational change for the poly[L‐Asp(OBzl)] copolymers was observed in the following composition ranges: L‐Leu, 0–15 mol %; L‐Ala, 0–32 mol %; L‐Val, 0–8 mol %; L‐Glu(OBzl), 3–10 mol %; and Cbz‐L‐Lys, 0–9 mol %.

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