HTL affects the chaperone activity of IDPs: A study based on α-casein and β-casein Mordhwaj1,*, Bhattacharya Reshmee2, Chandra Sulekh3, Singh Vandna1,** 1Department of School of Vocational Studies and Applied Sciences, Gautam Buddha University, Greater Noida, India 2Dr. B.R. Ambedkar Center for Biomedical Research (ACBR), University of Delhi, North Campus, India, reshmee93b@gmail.com 3Department of Chemistry, Zakir Husain Delhi College, University of Delhi, India, schandra_oo@yahoo.com *Corresponding Author E-mail: mordhwajanand@rediffmail.com
**malikvandna@gmail.com
Online published on 12 June, 2018. Abstract Several factors responsible for the Hcy-associated toxicity have been proposed and well documented, including oxidative stress, lipid peroxidation, neuronal degeneration and apoptosis. Post-translational modification of proteins by the Hcy metabolite, homocysteine-thiolactone (HTL), is one among the several proposed mechanisms of Hcyinduced toxicity. Incubation of proteins with HTL has been shown to form covalent adducts with protein lysine residues which ultimately results in structural and functional alterations. There has been an innumerable work done in understanding the role of N-homocysteinylation in globular proteins. However, in order to understand the effect of homocysteinylation in intrinsically disordered/unstructured proteins, alpha-and beta-casein proteins were used as model. Spectroscopic investigation revealed that HTL induces loss of chaperone activity. The study provides insights for the possible role of disorderness of IDPs for maintaining their biological activity. Top Keywords Homocysteine, Homocysteine-thiolactone, N-homocysteinylation. Top |