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Colloid and Polymer Science

, Volume 266, Issue 9, pp 783–792 | Cite as

Macromolecular conformations at the water-air interface: Interactions between alpha and beta conformations of polypeptides

  • P. Baglioni
  • L. Dei
  • G. Gabrielli
  • F. M. Innocenti
  • A. Niccolai
Polymer Science

Abstract

Bidimensional miscibility between alpha and beta conformations of polypeptides was investigated at the water-air interface in the 15°–30°C temperature range. The polypeptides were poly-γ-methyl-L-glutamate (PGMG), poly-γ-benzyl-L-glutamate (PGBG) and poly-γ-benzyl-L-aspartate (PBBA). The polypeptide conformations, alpha or beta, were checked by IR spectroscopy using the MIR technique.

The spreading isotherms for mixed monolayers alpha-PGMG/alpha-PGBG and beta-PGMG/beta-PBBA showed bidimensional miscibility both for alpha-alpha and beta-beta mixtures.

For the alpha-alpha system, attractive interactions among the polypeptide alphahelices were found (ΔGmix<0) and the driving factor appeared to be the entropic one (packing). Compressibility moduli and surface potential measurements showed a “fluidification” effect of alpha-PGBG on mixed monolayers. In the case of beta-beta mixed monolayers, ideal behaviour was observed and no “fluidification” effect detected.

Scanning electron micrographs made on collapsed monolayers showed hexagonal structures for alpha-alpha mixtures and no well-defined or characterized features for the beta-beta system.

Key words

Macromolecules air-water interface polypeptides macromolecular conformations monolayers 

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Copyright information

© Steinkopff 1988

Authors and Affiliations

  • P. Baglioni
    • 1
  • L. Dei
    • 1
  • G. Gabrielli
    • 1
  • F. M. Innocenti
    • 1
  • A. Niccolai
    • 1
  1. 1.Dipartimento di ChimicaUniversità degli Studi di FirenzeFirenzeItaly

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