About CCMB

Scientist Details

Contact Details

Name : N Madhusudhana Rao

Room : S106

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Research Interests

Chemistry and dynamics of a protein surface determines the half-life, stability, solvent- and protein- protein interactions. We employ random and knowledge based approaches to alter the surface amino acids to generate populations of interest. Using such methods we have evolved a lipase to melt at (Tm) at 780C from 560C and enhanced the binding o a ligand to lac repressor by 50 fold. Proteolytic stability, an important pharmaceutical property, is poorly correlated to structure and is currently being investigated. We spend considerable time to develop tools that aid in high-throughput screening. We are also interested in generating nanoparticulate materials based on peptides and lipids to enhance siRNA delivery. Peptide and protein interfacing to gold and iron oxide particles is being employed to develop methods for analyte and enzyme detection.

Selected Publications

  • Ahmad, S, Kamal, MZ, Sankaranarayanan, R and Rao, NM ( 2008) Thermostable Bacillus subtilis lipases: In vitro evolution and structural insight. JOURNAL OF MOLECULAR BIOLOGY 381,324-340.

  • Vijayalakshmi, A., Tarunashree, Y., Baruwati, B., Manorama, S. V., Narayana, B. L., Johnson, R. E. C. and Rao, NM (2008) Enzyme field effect transistor (ENFET) for estimation of triglycerides using magnetic nanoparticles. BIOSENSORS & BIOELECTRONICS 23, 1708 – 1714.

  • Acharya, P, Rajakumara, E, Sankaranarayanan, R and Rao, NM (2004) Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase. JOURNAL OF MOLECULAR BIOLOGY 341, 1271- 1281.

  • Rajagopalan, Rukkumani, Xavier, Jennifer, Rangaraj, Nandini , Rao, NM and Gopal, Vijaya (2007) Recombinant fusion proteins TAT-Mu, Mu and Mu-Mu mediate efficient non-viral gene delivery. JOURNAL OF GENE MEDICINE 9, 275-286.

  • Ahmad S, Rao NM 2009 Thermally denatured state determines refolding in lipase: Mutational analysis PROTEIN SCIENCE 18, 1183-1196

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