Secondary structure-improved bioaffinity correlation in elongated and modified synthetic epitope peptides from p24 HIV-1 core protein

摘要

In order to study the correlation between secondary structure and bioaffinity of long and modified sequences of p24 protein from HIV-1, three peptides containing the minimal size epitope from region 208-217 (EAAEWDRVHP) were prepared. It was found that peptide p24-1n, an elongated native sequence, has the lowest K_D and a predominant α-helix structure in the presence of trifluoroethanol. Three peptides containing another epitope from region 293-302 (FRDYVDRFK) were also synthesized. We have observed that modifications on the native sequence p24-2n (region 287-308) increased the α-helix content and this was correlated with an improvement of the recognition by antibodies in ELISA.