Sodium trichloroacetate-induced helical conformation of poly(l-lysine)

Sodium trichloroacetate which has been reported previously to be an effective denaturation reagent for proteins was applied to poly(l-lysine) and poly(l-glutamic acid) to see its effects on a coil-to-helix transition and on the chemical reactivities of the ε-amino group of poly(l-lysine). Addition of sodium trichloroacetate to poly-(l-lysine) induced a helical conformation even at neutral pH where the ε-amino group of the polymer was protonated. On the other hand, little effect was observed on the coil-to-helix transition of poly(l-glutamic acid). The ε-amino group of poly-(l-lysine) has an anomalously high reactivity with naphthoquinone 4,6-disulfonate carrying a negative charge. Sodium trichloroacetate inhibited the reaction of the ε-amino group with this reagent, while sodium trichloroacetate enhanced slightly the reaction of the ε-amino group of poly(l-lysine) with diazonium-1-H-tetrazole carrying a positive charge.