Anion-induced conformational transition of poly(l-arginine) and its two homologues

The interaction of various anions with poly(l-arginine) and its two homologues, poly(l-homoarginine) and poly(l-α-amino-γ-guanidinobutyric acid), has been studied in the neutral pH region. These polypeptides were found to change their conformations from coil to helix due to I^?, ClO^?₄ and SCN^?, and among them poly(l-homoarginine) and poly(l-arginine) were found to change conformation at smaller concentrations of the anions than poly(l-lysine). The helix of poly(l-homoarginine) was induced in the lyotropic series of the counteranions. Using the van't Hoff enthalpies for the transition of the polypeptides and the transition enthalpies obtained from calorimetry, the various thermodynamic parameters of the transitions were calculated by use of a theory based on the non-specific and the specific binding interactions of the anions with the charged sites on the polypeptides. The binding constants of ClO^?₄ and SCN^? with poly(l-homoarginine) and poly(l-arginine) were found to be four times as large as those with poly(l-lysine). The free energy changes of the transitions from coil to helix of poly(l-homoarginine) and poly(l-arginine) were found to be more negative than that of poly(l-lysine). From these results, the guanidinium ion can be concluded to form easily the ion pair with the anions on the polymer surface, thus allowing poly(l-homoarginine) and poly(l-arginine) to change their conformations at smaller concentrations of the anions than poly(l-lysine).