alpha,beta-dehydrophenylaianine containing cecropin-melittin hybrid peptides: conformation and activity

作者：Mathur Puniti; Jagannathan N R; Chauhan V S^*

来源：Journal of Peptide Science, 2007, 13(4): 253-262.

DOI：10.1002/pse.841

• dehydroamino acids
• bioactive peptides
• cecropin
• melittin
• antibiotic peptides

Synthesis and conformational studies of a cecropin-melittin hybrid pentadecapeptide CA(1-7)MEL(2-9), and its three alpha, beta-dehydrophenylalanine (Delta Phe) containing analogs in water-TFE mixtures are described. APhe is placed at strategic positions in order to preserve the amphipathicity of the molecule. The wild type CAMELO and its three analogs, containing one, two and three APhe residues namely CAMEL Delta Phe1, CAMEL Delta Phe2 and CAMEL Delta Phe3 respectively were synthesized in solid phase and their conformation determined by CD and NMR. CAMEL Delta Phe2 and CAMEL Delta Phe3 peptides exhibit the presence of 3(10)-helix and beta-turns in the former and only turns in the latter. CAMEL Delta Phe1 peptide was found to have a largely extended conformation. Antibacterial and hemolytic activities of the peptides were also evaluated. CAMEL Delta Phe2 peptide is maximally potent against both Staphylococcus aureus ATCC 259230 and Escherichia coli ATCC 11303. CAMEL Delta Phe1 with a single APhe at the center shows minimal hemolysis.

• 出版日期2007-4
• 单位河北医科大学