Abstract
The selected model polypeptides poly(Lys-Ala) and poly(Lys-Ala-Ala-Ala) underwent a helix-forming interaction with potassium pectates and pectinates of various esterification degree (E) and with some potassium oligogalacturonates (n = 2-5, 9, 13). Formation of the complex quantitatively monitored by a circular dichroic measurement showed that the specific band distribution of charged side chains of lysine units at the surface of helical structure does not constitute grounds for the local mode of interaction. Potassium pectinate of esterification degree E 57%, corresponding to polypeptides by charge density, does not reveal enhanced complexation values. The complex-forming efficacy continuously decreases with the increase of the esterification degree of pectin. Saturation of charges of the polypeptide was achieved predominantly by the spatial action of the superhelical structure of D-galacturonate chains.
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