Small heat shock proteins are critical for several cellular functions. Failure of heat shock proteins, thus, can cause compromised cellular activity leading to disease.
Our laboratory works on a number of small heat shock proteins such as HspB2, HspB3, HspB4 and B5 (Alpha A- and B-crystallins), hsp22 and hsp33. Point mutations (R116C in HspB4 and R120G in hsp5) are associated with congenital cataract and desmin related myopathy. We have shown that these point mutations lead to loss of chaperone-like activity. Loss of chaperone-like activity is associated with disease; restoring the activity with engineered proteins or small molecules should have therapeutical potential. We have engineered two proteins with enhanced activity. We also observed that a small molecule can improve the chaperone-like activity.
Fungal Keratitis is an eye dieses that can be treated with anti fungal drugs. Availability of the drug at the site of action is less than satisfactory. Some times cornea might be damaged compromising the vision. We have investigated fungal infection and consequent changes. We have identified a few biomolecules that might be of value in treating fungal keratitis, minimizing the corneal damage.
Born in Huzurabad, Andhra Pradesh, Mohan Rao has obtained his B.Sc. degree from the Arts and Science College (Osmania University), Warangal and M.Sc.(Physical Chemistry) form Kakatiya University, Warangal. Then he moved to the University of Hyderabad for a Ph.D. programme in chemistry. During the Ph.D. programme, he worked on photoacoustic spectroscopy of chemical and biological systems. This work also involved modification and improvement of the system, data acquisition and processing software.
Later he joined CCMB and initiated intact lens spectroscopic investigation. During 1990-92, he visited National Eye Institute of the National Institutes of Health, Bethesda, USA and carried out investigations on stability of crystallins and the role of nucleotides in the damage to eye lens due to exposure to ultraviolet light. On his return he initiated work on protein folding in health and disease, particularly molecular chaperone like property of alpha-crystallin and its relation to cataract, neurodegenerative diseases and cardiomyopathy. He is also investigating other heat-shock proteins such as hsp22 and hsp33.
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