UM Biophysics Faculty | A Ramamoorthy

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A Ramamoorthy

Structural Biology of Membranes

Membrane Disruption by antibiotics and nanomedicine

Solid-State NMR Spectroscopy

Ph.D. - Indian Institute of Technology, Kanpur, India

Dept: Associate Professor - Chemistry

Office Address: 4533 Chemistry

Phone: (734) 647-7623

Email: ramamoor@umich.edu

Research Group

Membrane proteins act as enzymes, regulate transport processes, and play a central role in intercellular communication. In order to understand the diverse functions of membrane proteins and to engineer these functions for biomedical or biotechnological purposes, it is necessary to determine their high-resolution structure and to describe their dynamics. Structure determination of membrane proteins continues to be one of the most important and challenging aspects of science at the present time. Recent developments in solid-state NMR spectroscopy have shown that it is an ideal technique for immobile and non-crystalline proteins that are difficult to study by X-ray crystallography or by solution NMR. The development of solid-state NMR methods and their applications to determine the structure, folding and dynamics of membrane proteins are the main goals of the research program. Solid-state NMR experiments on membrane proteins incorporated in oriented and unoriented phospholipid bilayers are performed to determine the structure of membrane proteins. Peptide antibiotics, human apolipoprotein, cytochrome b5, viral protein, functional fragments of GABA receptors, and amyloidogenic peptides are some of the systems currently under investigation by this group. High-resolution details on the membrane interaction of nanomedicine (or drug delivery), polymorphism of pharmaceutical compounds, and metabalomics are also being investigated using solid-state NMR experiments. We are also interested in studying protein-ligand (protein, peptide, or drug) interactions using a variety of biophysical techniques (CD, DSC, ITC, fluorescence, NMR and AFM).

AWARDS
NSF Career Development Award

Representative Publications

A. Ramamoorthy, S. Thennarasu, A. Tan, K. Gottipati, S. Sreekumar, D. L. Heyl, F. Y. P. An, and C. E. Shelburne, Deletion of all cycteines in Tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and LPS selective binding, Biochemistry, in press.

U. H. N. Dürr, U. S. Sudheendra, and A. Ramamoorthy, LL-37, the only human member of the cathelicidin family of antimicrobial peptides, BBA-Biomembranes, in press.

S. Dvinskikh, U. Duer, K. Yamamoto, and A. Ramamoorthy, A High Resolution Solid State NMR Approach for the Structural Studies of Bicelles, J. Am. Chem. Soc., 128, 6326 (2006).

F. Porcelli, B. Buck-Koehntop, S. Thennarasu, A. Ramamoorthy and G. Veglia, Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers by NMR spectroscopy, Biochemistry, 45, 5793-5799 (2006).

J. P. S. Powers, A. Tan, A. Ramamoorthy, and R. E. W. Hancock, Solution Structure and Interaction of the Antimicrobial Polyphemusins with Lipid Membranes, Biochemistry 44, 15504-15513 (2005).

A. Mecke, D. K. Lee, A. Ramamoorthy, B. G. Orr and M. M. B. Holl, Membrane thinning due to antimicrobial peptide binding: An atomic force microscopy study of MSI-78 in lipid bilayers, Biophys. J., 99, 4043-4050 (2005).

A. Mecke, D. K. Lee, A. Ramamoorthy, B. G. Orr and M. M. B. Holl, Synthetic and natural polycationic polymer nanoparticles interact selectively with fluid-phase domains of DMPC lipid bilayers, Langmuir 21, 8588-8590 (2005)

S. Thennarasu, D. K. Lee, A. Tan, U. P. Kari, and A. Ramamoorthy, Antimicrobial Actvity and Membrane Selective Interactions of a Synthetic Lipopeptide MSI-843, Biochim. Biophys. Acta, 1711, 49-58 (2005).

T. Narasimhaswamy, D. K. Lee, K. Yamamoto, N. Somanathan, and A. Ramamoorthy, A 2D Solid-State NMR Experiment to Resolve Overlapping Aromatic Resonances of Thiophene Based Nematogens, J. Am. Chem. Soc., 127, 6958-6959 (2005).

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