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STRUCTURE - FUNCTION CORRELATIONS IN PEPTIDE ANTIBIOTICS : Our research has been directed towards structure-function correlations in antibacterial peptides with the objectives of (i) delineating regions that could be important for activity and (ii) designing peptides ~15 residues or less that would have selective antimicrobial activity. Our results indicate that it is possible design membrane-active peptides with selective activity against bacteria and have therapeutic potential. INTRACELLULAR SORTING OF PROTEINS: multiple palmitoylation of cellular proteins controls many important cellular events. We have shown that peptides containing palmitoylation sites could serve as useful models for understanding the role of this intriguing modification in cell biology. SELF-ASSEMBLY PROCESS IN PEPTIDES AND PROTEINS :Our research in this area has shown that self-assembled structures of peptides with varying morphologies and electrical properties can be obtained by judicious choice of solvents for dissolution and surfaces for deposition.
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- Sitaram, N., and Nagaraj, R. (1999) Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity. Biochim Biophys Acta 1462, 29-54.Mandal, M., Jagannadham, M. V., and Nagaraj, R. (2002) Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs:structural and disulfide bridge requirements for activity. Peptides 23, 413-418.
- Pallavi, B., and Nagaraj, R. (2003) Palmitoylated peptides from the cysteine- rich domain of SNAP-23 cause membrane fusion depending on peptide length, position of cysteines, and extent of palmitoylation. J Biol Chem 278, 12737-12744.
- Sowmya, B. L., Jagannadham, M. V., and Nagaraj, R. (2006) Interaction of synthetic peptides corresponding to the scaffolding domain of Caveolin-3 with model membranes. Biopolymers 84, 615-624.
- Chaudhary, N., Singh, S., and Nagaraj, R. (2008) Organic solvent mediated self-association of an amyloid forming peptide from beta(2)-microglobulin: An atomic force microscopy study. Biopolymers 90, 783-791