Aggregation of globular protein as a consequences of macromolecular crowding: A time and concentration dependent study

Siddiqui, G.A. and Naeem, A. (2018) Aggregation of globular protein as a consequences of macromolecular crowding: A time and concentration dependent study. International Journal of Biological Macromolecules, 108. pp. 360-366. ISSN 1418130

Full text not available from this repository.
Official URL: http://www.sciencedirect.com/science/article/pii/S...

Abstract

The living cells show profoundly crowded condition, called as macromolecular crowding. Crowding essentially impacts on protein structure and lead to its aggregation. Protein aggregates have been involved in a wide range of diseases including Parkinson, Alzheimer's, and Huntington's. Increased in normal physiological macromolecular crowding because of increasing age can be implicated as one of the leading cause of proteopathies. In the present study, we have demonstrated the effect of macromolecular crowding on native structure of hemoglobin using bovine serum albumin as a crowding agent. Conformational changes of Hb at different concentrations of BSA were monitored using intrinsic fluorescence and ATR-FTIR spectroscopy. These results showed the transition of native Hb to a non-native form. Thermodynamic parameters were analyzed by isothermal titration calorimetry. The measurements of turbidity, thioflavin T, congo red and intrinsic fluorescence revealed the formation of significant protein aggregates with time. The kinetics of protein aggregation using relative ThT and 8-anilino-1-naphthalenesulphonic acid spectra clearly showed acceleration of the process with time and in concentration dependent manner. The spectra at 80 g/l of BSA incubated for 64 h showed formation of maximum Hb aggregates. Transmission electron microscopy results clearly showed the formation of amyloid aggregates structures, thus supporting the spectroscopic data. © 2017 Elsevier B.V.

Item Type: Article
Uncontrolled Keywords: Macromolecular crowding; Protein aggregates; Proteopathies
Divisions: Faculties > Faculty of Life Sciences > Department of Biochemistry
Depositing User: AMU Library
Date Deposited: 18 Jan 2018 09:59
Last Modified: 18 Jan 2018 09:59
URI: http://ir.amu.ac.in/id/eprint/10789

Actions (login required)

View Item View Item