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DOI10.1016/j.ijbiomac.2020.04.091
Structural stability and solubility of glycated camel lens zeta-crystallin
Abdullah, Ejlal Mohamed; Haq, Samina Hyder; Ahmed, Mohammed Asif; Khan, Javed Masood; Alamery, Salman Freeh; Malik, Ajamaluddin
通讯作者Malik, A
来源期刊INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
ISSN0141-8130
EISSN1879-0003
出版年2020
卷号158页码:384-393
英文摘要The camel has several biochemical, physiological, and anatomical features to withstand the harsh desert climate. Camel eye lens contains a novel protein (zeta-crystallin) in bulk quantity. Previous reports suggest that non-enzymatic glycation of eye lens proteins plays an important role in the etiology of cataract. In this study, we have characterized the role of glucose, fructose, and methylglyoxal (MGO) in the glycation of camel lens zeta-crystallin. From the results obtained, it was found that MGO reacted rapidly, fructose reacted moderately, and glucose was the least reactive even after prolonged incubation (N100 days). Glycation with MGO and fructose led to changes in the structure of zeta-crystallin, while glucose had no remarkable effect. The surface hydrophobicity did not change and no aggregates or amyloid fibrils were observed in the glycated zeta-crystallin. Moreover, the secondary structure of glycated zeta-crystallin remained similar after glycation. Our results suggested that due to natural adaptation, the camel lens protein zeta-crystallin retained its structure and solubility even after glycation to perform the single known function of the lens proteins: to focus unscattered light on the retina. (c) 2020 Elsevier B.V. All rights reserved.
英文关键词zeta-Crystallin Glycation Camel Methylglyoxal Eye lens Cataract
类型Article
语种英语
收录类别SCI-E
WOS记录号WOS:000564486400012
WOS关键词ALPHA-CRYSTALLIN ; NONENZYMATIC GLYCATION ; CATARACT DEVELOPMENT ; END-PRODUCTS ; EYE ; AGGREGATION ; PROTEINS ; GLUCOSE ; GLYCOSYLATION ; PURIFICATION
WOS类目Biochemistry & Molecular Biology ; Chemistry, Applied ; Polymer Science
WOS研究方向Biochemistry & Molecular Biology ; Chemistry ; Polymer Science
来源机构King Saud University
资源类型期刊论文
条目标识符http://119.78.100.177/qdio/handle/2XILL650/325915
作者单位[Abdullah, Ejlal Mohamed; Haq, Samina Hyder; Alamery, Salman Freeh; Malik, Ajamaluddin] King Saud Univ, Coll Sci, Dept Biochem, Bldg 5,Room 2A56,POB 2455, Riyadh 11451, Saudi Arabia; [Ahmed, Mohammed Asif; Khan, Javed Masood] King Saud Univ, Dept Food Sci & Nutr, Coll Food & Agr Sci, Riyadh 11451, Saudi Arabia
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Abdullah, Ejlal Mohamed,Haq, Samina Hyder,Ahmed, Mohammed Asif,et al. Structural stability and solubility of glycated camel lens zeta-crystallin[J]. King Saud University,2020,158:384-393.
APA Abdullah, Ejlal Mohamed,Haq, Samina Hyder,Ahmed, Mohammed Asif,Khan, Javed Masood,Alamery, Salman Freeh,&Malik, Ajamaluddin.(2020).Structural stability and solubility of glycated camel lens zeta-crystallin.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,158,384-393.
MLA Abdullah, Ejlal Mohamed,et al."Structural stability and solubility of glycated camel lens zeta-crystallin".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 158(2020):384-393.
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