Pharmaceutical acetylation can modulate the amyloidogenicity of human serum albumin

Bharathi, V. and Manglunia, R.R. and Sharma, N. and Nirwal, S. and Patel, Basant Kumar (2021) Pharmaceutical acetylation can modulate the amyloidogenicity of human serum albumin. Indian Journal of Biochemistry and Biophysics, 58 (4). pp. 344-351. ISSN 0301-1208

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Abstract

Human serum albumin (HSA) is an abundant carrier protein present in the blood plasma manifesting affinity for drugs and ligands. The bindings of several drugs can cause changes in the structural conformation of HSA that may affect its function. HSA is also known to in vitro form amyloid-like aggregates with fibrillar morphology as observed under TEM. Earlier, we showed that the HSA amyloid-like aggregates display self-seeding potential and detergent stability and the dimers of HSA, which are preferable for clinical applications due to their longer circulatory life, can also form amyloid-like aggregates. As aspirin, a commonly prescribed drug, was previously documented to acetylate HSA at one of its lysine residues, here, we examined if acetylation has any effect on the in vitro amyloid-like aggregation of HSA. We show that HSA acetylated in vitro using acetylsalicylic acid manifests relatively reduced levels of amyloid-specific properties such as turbidity, Thioflavin-T-positive aggregation, Î²-sheet content and stability against an ionic detergent. Also, TEM imaging shows that the acetylated HSA forms relatively less aggregates and with smaller sizes whereas, the aggregates of HSA are more abundant and larger in sizes with fibrillar morphology which further supports that acetylation can attenuate the amyloid-like aggregation of HSA. Â© 2021, National Institute of Science Communication and Information Resources. All rights reserved.

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IITH Creators:

IITH Creators	ORCiD
Patel, Basant Kumar	http://orcid.org/0000-0001-9465-4803

Item Type:

Article

Additional Information:

VB and RRM contributed equally to the work reported in this manuscript. We thank IIT Hyderabad funded by ministry of education, Govt. of India for research infrastructure and support. VB thanks DBT, Govt. of India, for senior research fellowship (SRF). RRM thanks ministry of education, Govt. of India for MTech fellowship. NS and SN thank ministry of education, Govt. of India for SRF. We thank Sri Amruthaa, IIT Hyderabad for help with TEM imaging.

Uncontrolled Keywords:

Acetylation, Human serum albumin, Sarkosyl, Thioflavin-T

Subjects:

Others > Biotechnology

Divisions:

Department of Biotechnology

Depositing User:

. LibTrainee 2021

Date Deposited:

13 Sep 2022 07:24

Last Modified:

13 Sep 2022 07:24