Isomeric Peptides: Diverse Functions

Sasmal, Supriya (2014) Isomeric Peptides: Diverse Functions. Masters thesis, Indian Institute of Science Education and Research Kolkata.

PDF (MS dissertation of Supriya Sasmal) Supriya_Sasmal_12ip003.pdf - Submitted Version Restricted to Repository staff only Download (2MB)

Abstract

Moleculer recognition and self-assembling peptides can fabricate diverse supramolecular architectures like supramolecular helix, supramolecular sheets and others, which have potential importance in biological as well as material sciences. Previous studies suggested that isomeric peptides can adopt different structures. In this regards, three isomeric hybrid peptides have been designed and synthesized which can self-assemble to form various supramolecular architectures. The chapter 3 entitled “Structure and function of isomeric hybrid dipeptides” represents synthesis of a series of hybrid dipeptides containing N-terminal L-tyrosine and C-terminal rigid aromatic β/ γ/ δ amino acids by solution phase methods, their characterization by NMR, FTIR and Mass spectroscopy, their morphological studies by Field Emission Scanning Electron Microscopy. The solution study exhibits that the peptides have different backbone conformations and aggregation pattern. The solid state FTIR exhibits that the peptides are extensively hydrogen bonded. The CD study shows that peptide 1 adopt a sheet-like structure. But Peptide 2 and 3 adopt helical structures. Moreover, the peptide 1 binds with an anti cancer drug nicotinamide. The peptide 2 forms organogel in cyclohexane at low temperature. The xerogel exhibits nano crystal entangled morphology.

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