Incorporation of α-methylated amino acids into Apolipoprotein A-I mimetic peptides improves their helicity and cholesterol efflux potential.

ABSTRACT: Apolipoprotein A-I (ApoA-I) mimetic peptides are potential therapeutic agents for promoting the efflux of excess cellular cholesterol, which is dependent upon the presence of an amphipathic helix. Since α-methylated Ala enhances peptide helicity, we hypothesized that incorporating other types of α-methylated amino acids into ApoA-I mimetic peptides may also increase their helicity and cholesterol efflux potential. The last helix of apoA-I, peptide 'A' (VLESFKVSFLSALEEYTKKLNT), was used to design peptides containing a single type of α-methylated amino acid substitution (Ala/A_α, Glu/D_α, Lys/K_α, Leu/L_α), as well as a peptide containing both α-methylated Lys and Leu (6_α). Depending on the specific residue, the α-helical content as measured

SUBMITTER: Islam R 

PROVIDER: S-EPMC8482877 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature