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.
