Background: In spite of current progress in treatment methods, cancer is a major source of
morbidity and death rate all over the world. Traditional chemotherapeutic agents aim to divide cancerous
cells, are often associated with deleterious side effects to healthy cells and tissues. Host defense peptides
Cecropin A and B obtained from insects are capable to lyses various types of human cancer cells at peptide
concentrations which are not fatal to normal eukaryotic cells.
Methods: In the present work we have designed short chain α-helical linear and cyclic peptide from cecropin
A having same cationic charge, hydrophobicity and helicity. Synthesis of designed novel short chain
linear (10) and cyclic compound (12) was accomplished by using solution phase method. All the coupling
reactions were carried out by using dicyclohexylcarbodiimide (DCC) as the coupling reagent at room temperature
in the presence of N-methylmorpholine (NMM) as the base. The Structure of newly synthesized
peptidse were elucidated by 1H-NMR, 13C-NMR, FT-IR, FABMS and elemental analysis data.Cytotoxicity
of synthesized compound was tested against Dalton’s Lymphoma Ascites (DLA), Ehrlich’s Ascites
Carcinoma (EAC) and MCF-7 cell lines by using MTT assay and 5-FU as reference compound.
Result: From biological assessment,it was found that short chain cyclicpeptide12 showed high level of
cytotoxic activity against DLA and EAC cell lines.
Conclusion: By utilizing a structure-based rational approach to anticancer peptide design from cecropin
A, we were able to develop short chain linear and cyclic peptides having same charge, hydrophobicity
and with improved activity. Systematically removing amino acids, we were able to retaining peptide
charge and hydrophobicity/hydrophilicity in linear and cyclic peptide which results to optimize the anticancer
activity against DLA and EAC cell lines.