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Sequence peptide polymers: Part 2. Poly(leucyl-leucyl-aspartic acid)—Conformational aspects in water solution

Authors
Journal
Polymer
0032-3861
Publisher
Elsevier
Publication Date
Volume
13
Issue
11
Identifiers
DOI: 10.1016/0032-3861(72)90068-7
Disciplines
  • Physics

Abstract

Abstract A new sequential peptide, poly(leucyl-leucyl-aspartic acid) has been synthesized and the conformational properties in water have been examined by spectroscopic methods at different degrees of neutralization of the β-carboxyls of the aspartate residues and by potentiometric measurements. The experimental data are in agreement with the presence of α-helical segments stabilized by strong hydrophobic interactions. The calculation of the thermodynamic functions, ΔG 0, ΔH 0, ΔS 0 related to the transition uncharged random coil to uncharged α-helical state, gives at 25°C the following values: ΔG 0=−1575 cal/mol; ΔH 0=6173cal/mol; ΔS 0=26·0cal/deg mol. These values are expressed in cal/mol of repeating unit. The temperature dependence of the ellipticity and the function pH—log[ α (1−α) ] versus α, allows us to analyse the conformational stability of poly(leucyl-leucyl-aspartic acid).

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