Substituted benzenediol Schiff bases as promising new anti-glycation agents

Choudhary, M. Iqbal; Abbas, Ghulam; Ali, Saqib; Shuja, Shaukat; Khalid, Nasir; Khan, Khalid Mohammed; Atta-ur-Rahman, _; Basha, Fatima Z.

doi:10.3109/14756361003733621

Cited by 19 publications

(9 citation statements)

References 21 publications

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“…The half-life for collagen has been reported on the order of decades in healthy tissues (Bank et al, 1999; Maroudas et al, 1992; Verzijl et al, 2000b). Due to the long protein half-life in vivo , collagen is one of the proteins that undergo spontaneous glycation and the formation of measurable amounts of Advanced Glycation End products (AGEs) during aging (Choudhary et al, 2011; Sell and Monnier, 2004; Verzijl et al, 2000a; Verzijl et al, 2000b). …”

Section: Introductionmentioning

confidence: 99%

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

2014

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Recent molecular modeling data using collagen peptides predicted that mechanical force transmitted through intermolecular cross-links resulted in collagen triple helix unwinding. These simulations further predicted that this unwinding, referred to as triple helical microunfolding, occurred at forces well below canonical collagen damage mechanisms. Based in large part on these data, we hypothesized that mechanical loading of glycation cross-linked tendon microfibers would result in accelerated collagenolytic enzyme damage. This hypothesis is in stark contrast to reports in literature that indicated that individually mechanical loading or cross-linking each retards enzymatic degradation of collagen substrates. Using our Collagen Enzyme MechanoKinetic Automated Testing (CEMKAT) System we mechanically loaded collagen-rich tendon microfibers that had been chemically cross-linked with sugar and tested for degrading enzyme susceptibility. Our results indicated that cross-linked fibers were >5 times more resistant to enzymatic degradation while unloaded but became highly susceptible to enzyme cleavage when they were stretched by an applied mechanical deformation.

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Section: Introductionmentioning

confidence: 99%

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

2014

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“…For the past few years, studies of the coordination chemistry of thiosemicarbazone involved complexes with transition metal ions [6][7][8][9]. The synthesis and characterization of organotin(IV) complexes of Schiff base ligands have always attracted the attention of inorganic chemists and is well established in the literature [10][11][12][13][14]. Organotin(IV) complexes have been extensively studied due to their beneficial biological activities as well as their wide industrial and agricultural applications [15][16][17][18][19][20][21].…”

Section: Introductionmentioning

confidence: 99%

Organotin(IV) complexes of 2-hydroxyacetophenone-N(4)-cyclohexylthiosemicarbazone (H2dact): Synthesis, spectral characterization, crystal structure and biological studies

Affan

Salam

Ahmad

et al. 2012

Inorganica Chimica Acta

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Sn NMR spectral studies. The molecular structure of complex (5) has also been determined by single-crystal X-ray diffraction. The crystal structure of complex (5) showed that the ligand is doubly deprotonated at the oxygen and sulfur atoms and is coordinated to the tin(IV) atom through thiolate-S, azomethine-N and phenoxide-O atoms. X-ray diffraction studies indicated that complex (5) is a monomer and the central tin(IV) atom is five coordinated in a distorted trigonal bipyramidal geometry. The cytotoxicity of the ligand (1) as well as its organotin(IV) complexes (2-5) was studied against Artemia salina. The in vitro antibacterial activities of these compounds were also evaluated. The screening results have shown that the organotin(IV) complexes (2-5) have better antibacterial activity than the free ligand. Furthermore, it has been shown that diphenyltin(IV) derivative (5) exhibits significantly better activity than the monoorganotin(IV) derivatives (2-4).

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“…Glycation is the non-enzymatic combination of sugar molecule with protein amino acid or lipid resulting product is called advanced glycation endproducts (AGEs). The over expression of AGEs are believed to implicating in patients with diabetes and aging especially diabetes related late complications such as cataract, neuropathy, nephropathy, wound healing, Alzheimer's disease 28,37 arterial stiffness and decreased myocardial compliance, resulting from the loss of collagen elasticity. Agents that interfere with the formation of AGEs are targeting to be beneficial therapeutic tool for effective management of such conditions.…”

Section: Resultsmentioning

confidence: 99%

Isolation of a new bioactive cinnamic acid derivative from the whole plant of Viola betonicifolia

Muhammad

Saeed

Adhikari

et al. 2012

Journal of Enzyme Inhibition and Medicinal Chemistry

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Substituted benzenediol Schiff bases as promising new anti-glycation agents

Cited by 19 publications

References 21 publications

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

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

Organotin(IV) complexes of 2-hydroxyacetophenone-N(4)-cyclohexylthiosemicarbazone (H2dact): Synthesis, spectral characterization, crystal structure and biological studies

Isolation of a new bioactive cinnamic acid derivative from the whole plant of Viola betonicifolia

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