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Interactions between Charged Polypeptides and Nonionic Surfactants

Helen Sjögren ^* , Caroline A. Ericsson ^*, Johan Evenäs  and Stefan Ulvenlund ^* 

^* Physical Chemistry 1, Lund University, Lund, Sweden; and Medicinal Chemistry and Product Development, AstraZeneca R&D Lund, Lund, Sweden

Correspondence: Address reprint requests to Stefan Ulvenlund, Product Developoment, AstraZeneca R&D Lund, 221 87 Lund, Sweden. Fax: 46-46-337128; E-mail: stefan.ulvenlund{at}astrazeneca.com.

The influence of molecular characteristics on the mutual interaction between peptides and nonionic surfactants has been investigated by studying the effects of surfactants on amphiphilic, random copolymers of -L-amino acids containing lysine residues as the hydrophilic parts. The hydrophobic residues were either phenylalanine or tyrosine. The peptide-surfactant interactions were studied by means of circular dichroism spectroscopy and binding isotherms, as well as by 1D and 2D NMR. The binding of surfactant to the peptides was found to be a cooperative process, appearing at surfactant concentrations just below the critical micellar concentration. However, a certain degree of peptide hydrophobicity is necessary to obtain an interaction with nonionic surfactant. When this prerequisite is fulfilled, the peptide mainly interacts with self-assembled, micelle-like surfactant aggregates formed onto the peptide chain. Therefore, the peptide-surfactant complex is best described in terms of a necklace model, with the peptide interacting primarily with the palisade region of the micelles via its hydrophobic side chains. The interaction yields an increased amount of -helix conformation in the peptide. Surfactants that combine small headgroups with a propensity to form small, nearly spherical micelles were shown to give the largest increase in -helix content.