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Antiglycation potential of metal ions and polyphenolic extract of chickpea on thiol-protease inhibitor: A management for diabetic complications.
Shahnawaz Khan, Mohd; Ahmad Bhat, Sheraz; Saud Albagmi, Monnera; Arshad, Mohammed; Tarique, Mohammad; Bano, Bilqees.
Afiliación
  • Shahnawaz Khan M; Department of Biochemistry, College of Science, King Saud University, Riyadh, 11451, Saudi Arabia.
  • Ahmad Bhat S; College of Science, Cluster University Srinagar, INDIA.
  • Saud Albagmi M; Department of Biochemistry, College of Science, King Saud University, Riyadh, 11451, Saudi Arabia.
  • Arshad M; Dental Health Department, College of Applied Medical Sciences, King Saud University, Riyadh, Saudi Arabia.
  • Tarique M; Department of Child Health, School of Medicine, University of Missouri, Columbia, MO 65201, USA.
  • Bano B; Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, INDIA.
Saudi Pharm J ; 32(1): 101916, 2024 Jan.
Article en En | MEDLINE | ID: mdl-38178850
ABSTRACT
Glycation is the non-enzymatic adduct formation between reducing sugars or dicarbonyls with proteins and is a crucial molecular event under hyperglycaemic conditions of diabetes. The accumulation of advanced glycation end products (AGEs) due to glycation of proteins has been implicated in several diseases associated with ageing and diabetes. Thus, investigating the antiglycation potential of some trace metal ions (Manganese; Mn2+, and Zinc; Zn2+) and polyphenolic extract of chickpea seeds (PEC) on the methylglyoxal (MGO) induced glycation of a phytocystatin isolated from chickpea was taken up to find an inexpensive and non-toxic therapeutic means of medicating protein glycation and associated diabetic complications. The current study focused on the comparative analyses of these micronutrients and herbal extracts in inhibiting protein glycation and AGEs formation in a quest to develop nutraceuticals for managing diabetes. The effect of metals (Mn2+, Zn2+) and PEC on protein glycation was assessed by different techniques, i.e., glycation-specific AGE fluorescence and absorbance, thiol protease inhibitory activity assay, and conformational alterations by spectroscopic assays. This study revealed the significant anti-glycation potencies of Mn2+, Zn2+, and PEC against the MGO-induced glycation of CPC, which might pave the way for resolving pathological complications of diabetes by combining higher levels of efficacy, selectivity, and safety in humans. Moreover, characterization and identification of different AGEs formed during the glycation process in diabetics was done to apply the same for determining the onset of glycation at the early stage so that appropriate steps be taken to address the menace of diabetic complications.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: Saudi Pharm J Año: 2024 Tipo del documento: Article País de afiliación: Arabia Saudita

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: Saudi Pharm J Año: 2024 Tipo del documento: Article País de afiliación: Arabia Saudita