New insights into in vitro amyloidogenic properties of human serum albumin suggest considerations for therapeutic precautions

Sharma, N and Vishwanath, S and Maurya, S and Prasad, A and Khandelwal, P and Yadav, S C and Patel, Basant Kumar (2015) New insights into in vitro amyloidogenic properties of human serum albumin suggest considerations for therapeutic precautions. FEBS Letters, 589 (24P-B). pp. 4033-4038. ISSN 0014-5793

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Abstract

Amyloid aggregates display striking features of detergent stability and self-seeding. Human Serum Albumin (HSA), a preferred drug-carrier molecule, can also aggregate in vitro. So far, key amyloid properties of stability against ionic detergents and self-seeding, are unclear for HSA aggregates. Precautions against amyloid contamination would be required if HSA aggregates were self-seeding. Here, we show that HSA aggregates display detergent sarkosyl stability and have self-seeding potential. HSA dimer is preferable for clinical applications due to its longer retention in circulation and lesser oedema owing to its larger molecular size. Here, HSA was homodimerized via free cysteine-34, without any potentially immunogenic cross-linkers that are usually pre-requisite for homodimerization. Alike the monomer, HSA dimers also aggregated as amyloid, necessitating precautions while using for therapeutics.

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IITH Creators:
IITH CreatorsORCiD
Patel, Basant Kumarhttp://orcid.org/0000-0001-9465-4803
Item Type: Article
Uncontrolled Keywords: HSA amyloid; Self-seeding; Plasma expander; Drug carrier; Sarkosyl
Subjects: Others > Biotechnology
Divisions: Department of Biotechnology
Depositing User: Team Library
Date Deposited: 12 Nov 2015 06:43
Last Modified: 10 Nov 2017 06:39
URI: http://raiithold.iith.ac.in/id/eprint/2013
Publisher URL: https://doi.org/10.1016/j.febslet.2015.11.004
OA policy: http://www.sherpa.ac.uk/romeo/issn/0014-5793/
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