Literature DB >> 20583858

Substituted benzenediol Schiff bases as promising new anti-glycation agents.

M Iqbal Choudhary1, Ghulam Abbas, Saqib Ali, Shaukat Shuja, Nasir Khalid, Khalid M Khan, Fatima Z Basha.   

Abstract

A feature of diabetes is that the rate of protein glycation and the formation of advanced glycation endproducts (AGEs) increases spontaneously due to the abnormally elevated levels of sugar in the blood. The glycation of proteins is associated with a large number of late diabetic complications (retinopathy, neuropathy, atherosclerosis, end stage renal diseases, rheumatoid arthritis and neurodegenerative diseases). The increase in diabetic complications is a major cause of morbidity and mortality, which has increased significantly in the last two decades. Therefore, there is a considerable recent interest in the identification of lead molecules, which can inhibit the glycation process or slow it down considerably. A new class of anti-glycation agents has been identified, based on the spectrofluorimetric analysis of fluorescent advanced glycation endproducts (AGEs), benzenediol Schiff bases, and their structure-activity relationships have been studied. Some of these compounds have shown a promising anti-glycation potential in vitro.

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Year:  2010        PMID: 20583858     DOI: 10.3109/14756361003733621

Source DB:  PubMed          Journal:  J Enzyme Inhib Med Chem        ISSN: 1475-6366            Impact factor:   5.051


  2 in total

1.  Glycation cross-linking induced mechanical-enzymatic cleavage of microscale tendon fibers.

Authors:  Jonathan W Bourne; Jared M Lippell; Peter A Torzilli
Journal:  Matrix Biol       Date:  2013-12-04       Impact factor: 11.583

2.  Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide.

Authors:  Patrick Bogdanowicz; Marie-José Haure; Isabelle Ceruti; Sandrine Bessou-Touya; Nathalie Castex-Rizzi
Journal:  Clin Cosmet Investig Dermatol       Date:  2016-06-22
  2 in total

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