Conformational Studies of Gramicidin Inspired Alternating LD Peptides

Kumar, Pratik (2013) Conformational Studies of Gramicidin Inspired Alternating LD Peptides. Masters thesis, Indian Institute of Science Education and Research Kolkata.

PDF (BS MS Dissertation of Pratik Kumar (08MS52)) Pratik_Kumar_08MS52_MSThesis.pdf - Submitted Version Restricted to Repository staff only Download (2MB)

Abstract

The conformational properties of polypeptides are of great interest to structural biologists and chemists for their functional significance. Several peptide antibiotics, like Gramicidin, Valinomycin are having D-amino acids in the sequence. Gramicidins are linear pentadecapeptide antibiotics produced by the soil bacterium Bacillus brevis during sporulation. It consists of alternating L- and D-amino acids, in contrast to most natural peptides or proteins, which are made of L-amino acids. Gramicidin acts as an ion channel in bacterial cell membrane allowing monovalent cations (K+, Na+) travel from extracellular environment to the cytoplasm. It forms beta helical structure inside lipid bilayer and dimerizes to span the whole membrane. This thesis attempts to explore the conformational properties of gramicidin-inspired alternating L- and D-amino acids containing polypeptides.

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