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.
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Baglioni, P., Dei, L., Gabrielli, G. et al. Macromolecular conformations at the water-air interface: Interactions between alpha and beta conformations of polypeptides. Colloid & Polymer Sci 266, 783–792 (1988). https://doi.org/10.1007/BF01417862
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DOI: https://doi.org/10.1007/BF01417862