Synthesis of esculentin-1 antibacterial peptide fragments on 1,4-butanediol dimethacrylate cross-linked polystyrene support

Peptide segments corresponding to antibacterial esculentin-1 (1-15), (33-44 ), (9-27), and their modified forms were synthesized on 1,4-butanediol dime thacrylate cross-linked polystyrene (PS-BDODMA) support. Hydroxymethyl and aminomethyl 2% PS-BDODMA supports were used for the synthesis. The HMPB lin ker was appended to the aminomethyl resin using HBTU in presence of HOBt an d the first amino acid was incorporated using MSNT. The conventional Fmoc s ynthetic protocol was used for the synthesis of peptides. The peptides were cleaved from the support using TFA. The peptides were purified by HPLC, an d characterized by amino acid analysis and MALDI TOF MS. The secondary stru ctures of the peptides were revealed by CD measurements. The synthesis of t hese peptides illustrates the utility of the new support for the synthesis of long-chain bioactive peptides. The synthetic peptides were tested for an timicrobial activity against Escherichia coli Mos blue, E. coli 2, Bacillus brevis, B. megaterium, Pseudomonas HTL, and Vibrio mimicus. The antibacter ial activity of the peptides was explained on the basis of the helicity and charged nature of the sequences.