ISSN: 2157-7064
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Asokan C
Sokoto State University, Nigeria
Scientific Tracks Abstracts: J Chromatogr Sep Tech
�±B-Crystallin is one of the heat shock proteins and its Chaperonic activity is well established. �±-Crystallin forms complexes with denaturing proteins thereby preventing their uncontrolled aggregation. Chaperonine process has been shown to follow a saturation type of complexing, when the ability of the available �±B-Crystallin to bind the target protein is exceeded, the excess target protein aggregates and eventually precipitates out of solution. The �±-Crystallin fractions are purified by HPLC and confirmed used for the study. The effect of �±B-Crystallin on A�± fibril formation under systemic amyloidodsis in the brain, we have determined they interact with each other. In the present study, in-vitro and in-vivo studies on the role of the interaction of SAA/SAA fibrils with chaperones were investigated. The results indicated that there was interaction between SAA and �±B-Crystallin; A�² and �±B-Crystallin when they were incubated together. A possible mechanism for this interaction and its implicated significance in-vivo study has shown �±B-Crystallin as a therapeutic use for amyloid disease.
Asokan C has completed his PhD from University of Madras and Postdoctoral studies from Columbia University. NY. USA. He is the Associate Professor, Department of Biochemistry, Sokoto State University, Sokoto. Nigeria. He has published more than 36 papers in reputed journals and has been serving as an Editorial Board Member of repute.
Email: asokan_74@hotmail.com