Design, Synthesis and Characterization of α-β Short Peptides as Bio-Active Molecules

Abstract

Being less toxic and specific peptide therapeutics represent advanced biological activities, but low oral-bioavailability and enzymatic degradation limit their applications. To supress limitations, peptide sequence obtained from milk-protein was modified into its β-analogue by synthesizing hybrid -β peptide. Synthesized -β alternative peptide sequence exhibits stability in aqueous media and resistance against proteolytic degradation. Using liquid phase synthesis -Gly-β-Leu, -Ser-β-Leu and -Tyr--Gly-β-Leu peptides were synthesized. Synthesis began with the NBoc/ O-Bn protective strategy and conversion of -amino acid into β-amino acid was accomplished by Arndt-Eistert homologation followed by subsequent Wolff-rearrangement with retention of configuration. EDC and HOBt were used in combination for coupling of amino acids without racemization. Synthesized -β peptide sequences were subjected to spectroscopic analysis and characterized by FTIR, NMR and CHNS. Further biological properties of desired peptides were investigated.