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Announcement
Announcement
To Study the activity of modified antimicrobial peptides

Student name: Ms Vanndita Bahl
Guide: Dr Ramakrishnan Sitaraman
Year of completion: 2015
Host Organisation: National Institute of Immunology, New Delhi
Supervisor (Host Organisation): Dr Kanwaljeet Kaur
Abstract: Antimicrobial peptides are ubiquitous molecules that are responsible for the innate immune response of the body and have shown to be effective against multi-drug resistant bacteria. Amphipathic in nature, these peptides show a large structural diversity and they adopt various mechanisms to kill the pathogens. The present study has been done on Tritrpticin, a natural AMP present in porcines (pig family). This 13 amino acid long palindromic peptide (VRRFPWWWPFLRR) has a high arginine (30%) and tryptophan (23%) content, and possesses a net positive charge. The peptide also shows a broad spectrum activity against gram-positive and gram negative bacteria. The present work has been carried out to study the activity of tritrpticin and its analogues. The different analogues of the peptide were synthesized by Solid Phase Peptide Synthesis using Fmoc chemistry by replacing tryptophan residues with tyrosine and serine residues at different positions. The peptides were modified to understand the effect of the tryptophan ring on the antimicrobial activity of the peptides. The Minimum inhibitory concentration assay was done using these peptides over a range of gram positive and gram negative bacteria and their activities were compared. It was observed that the MIC of serine and tyrosine analogues against various bacterial strains were nearly comparable and the native peptide without any modification was the most efficient in killing bacteria at lower concentrations. Also, cytotoxicity studies of all the peptides was done by MTT assay on macrophage J774 cell line which have showed that all the three serine analogues were less toxic mammalian cell lines in comparison to native tritrypticin and tyrosine analogues. Key words: Antimicrobial peptides, Fmoc, Tritrpticin, MIC, cytotoxicity.