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Pharmaceutical acetylation can modulate the amyloidogenicity of human serum albumin

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Title Pharmaceutical acetylation can modulate the amyloidogenicity of human serum albumin
 
Creator Bharathi, Vidhya
Manglunia, Ruchi Rajkumar
Sharma, Neetu
Nirwal, Sadhana
Patel, Basant K
 
Subject Acetylation
Human serum albumin
Sarkosyl
Thioflavin-T
 
Description 344-351
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, -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.
 
Date 2021-07-30T04:18:21Z
2021-07-30T04:18:21Z
2021-08
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://nopr.niscair.res.in/handle/123456789/57785
 
Language en
 
Publisher NIScPR-CSIR, India
 
Source IJBB Vol.58(4) [August 2021]