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Rosmarinic acid restrains protein glycation and aggregation in human serum albumin: Multi spectroscopic and microscopic insight - Possible Therapeutics Targeting Diseases
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Rosmarinic acid restrains protein glycation and aggregation in human serum albumin: Multi spectroscopic and microscopic insight - Possible Therapeutics Targeting Diseases

Anas Shamsi, Azaj Ahmed, Mohd Shahnawaz Khan, Fohad Mabood Husain and Bilqees Bano
International journal of biological macromolecules, Vol.161, pp.187-193
10/15/2020
DOI: 10.1016/j.ijbiomac.2020.06.048
PMID: 32526295

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Abstract

Protein aggregation and glycation are directly associated with many pathological conditions including several neurodegenerative disorders. This study investigates the potential of naturally occurring plant product, Rosmarinic acid (RA), to inhibit the glycation and aggregation process. In this study, we report that varying concentrations of methylglyoxal (MG) induce advanced glycation end products (AGEs) and aggregates formation in HSA in vitro on day 6 and day 8, respectively. AGEs specific fluorescence confirmed the formation of AGEs in HSA in the presence of MG and further characterized the inhibitory potential of RA. It was found that the presence of RA prevented AGEs formation in vitro. Further, aggregates of HSA were characterized employing multi spectroscopic and microscopic techniques and RA was found to inhibit this process. This study proposes that RA could be a potential natural molecule to treat disorders where AGEs and aggregates of proteins play a pivotal role. (C) 2020 Elsevier B.V. All rights reserved.
Biochemistry & Molecular Biology Chemistry Chemistry, Applied Life Sciences & Biomedicine Physical Sciences Polymer Science Science & Technology

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