| Abstract
| - Results of molecular dynamics simulations of different stoichiometric complexes constituted by poly(α,l-glutamate) and oppositely charged amphiphilic surfactants (n-hexylammonium, n-dodecylammonium,n-hexyltrimethylammonium and n-dodecyltrimethylammonium) are presented. Simulations were performedin dilute chloroform solution using explicit solvent molecules. It is shown that the conformation of thepolypeptide chain is strongly influenced by the constitution of the surfactant polar headgroup. Thus, thepolypeptide adopts a canonical α-helix conformation in complexes containing n-alkyltrimethylammoniumsurfactants, while a nonregular but also elongated conformation was found in complexes formed byalkylammonium surfactants. The latter structure is due to the interaction of alkylammonium cations withthe amide group of the polypeptide chain. On the other hand, we show the intrinsic tendency of themolecular cations to form multiple interactions with the polypeptide chain, independently of theirconstitution.
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