Circular dichroism studies on synthetic signal peptides

Abstract

Circular dichroism studies on synthetic peptides corresponding to the signal sequences of chicken lysozyme and Escherichia coli proteins, λ-receptor and lipoprotein, have been carried out in trifluoroethanol. The peptides, (CH₃)₃-C-O-CO-Thr-Leu-Lys-Lys-Leu-Pro-Leu-Ala-Val-Ala-Val-Ala-Ala-Gly-Val-Met-Thr-Ala-Ala-Met-Ala-OCH₃, (CH₃)₃-C-O-CO-Met-Lys-Ser-Leu-Leu-Ile-Leu-Val-Leu-Cys(benzyl)-Phe-Leu-Pro-Leu-Ala-Ala-Leu-Gly-OH and (CH₃)₃-C-O-CO-Leu-Val-Leu-Gly-Ala-Val-Ile-Leu-Gly-Thr-Thr-Leu-Leu-Ala-Gly-OCH₃, corresponding to the signal sequences of λ-receptor, lysozyme and the hydrophobic region of lipoprotein, respectively, show two negative bands at approx. 205 and 200 nm, characteristic of an a-helical conformation. Secondary structural features are discernible even in the shorter, 12-residue carboxy-terminal fragments of these signal peptides. A comparison of the conformation of the amino-terminal, central and carboxy-terminal fragments of lipoprotein signal sequence indicates that the central octapeptide fragment is more structurally ordered compared to the amino- and carboxy-terminal fragments.