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Disaggregation of amyloid-like protein aggregates isolated from human cataractous lens

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Title Disaggregation of amyloid-like protein aggregates isolated from human cataractous lens
 
Creator Mittal, Chandrika
Harsolia, Ram Swaroop
Singh, Manish
Yadav, Jay Kant
 
Subject Amyloids
Cataract
Crystallin
Disaggregation
Sodium dodecyl sulphate
 
Description 359-365
Crystallins, which represent the major lens protein, play a significant role in ensuring the lens transparency and
maintenance of appropriate refractive index of the lens that help in accurate focusing of incident visible light precisely on
retina to create clear image perception. Aggregation of lens proteins is known to form the basis of cataract formation. The
present study is an attempt to examine the stability of the lens protein aggregates, isolated from human cataract eye lens,
against an anionic detergent Sodium dodecyl sulphate (SDS), which is known to disrupt the hydrophobic interaction of
protein aggregates. Data that emerged from Congo red (CR), thioflavin T (ThT) and 8-anilino-1-naphthalene sulfonic acid
(ANS) binding assay indicated their amyloidogenic nature. A significant reduction in the bathochromic shift of CR λmax and
ThT fluorescence emission intensity were observed after treatment of the aggregated proteins with SDS. In the presence of
SDS, a significant change in the number and size of the protein aggregates were observed during their morphological
analyses under transmission electron microscopy (TEM). Based on the above data it became evident that the hydrophobic
interaction plays a crucial role in formation and stabilizing the protein aggregates during cataract formation.
 
Date 2021-07-30T04:14:37Z
2021-07-30T04:14:37Z
2021-08
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://nopr.niscair.res.in/handle/123456789/57783
 
Language en
 
Publisher NIScPR-CSIR, India
 
Source IJBB Vol.58(4) [August 2021]