Kinetics of inhibition of type I collagenase by dialdehyde cellulose in stabilization of type I collagen / Gladstone Christopher Jayakumar in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CX, N° 3 (03/2015)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CX, N° 3 (03/2015) . - p. 72-79 Titre : Kinetics of inhibition of type I collagenase by dialdehyde cellulose in stabilization of type I collagen Type de document : texte imprimé Auteurs : Gladstone Christopher Jayakumar, Auteur ; Nagarajan Usharani, Auteur ; Arjunan Yasothai, Auteur ; Swarna Vinodh Kanth, Auteur ; Jonnalagadda Raghava Rao, Auteur Année de publication : 2015 Article en page(s) : p. 72-79 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Antienzymes Cellulose dialdéhyde Collagénases Les collagénases sont des enzymes capables de rompre les liaisons peptidiques du collagène. Elles facilitent la destruction des structures extracellulaires lors de la pathogenèse bactérienne. Ce sont des exotoxines. La production de collagénases peut être induite lors d'une réponse immunitaire, par les cytokines qui stimulent les cellules telles que les fibroblastes et les ostéoplastes et occasionnent indirectement des lésions tissulaires. Collagène -- Stabilité Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Collagen is one of the widely studied biomaterial for various industrial applications. However, search of eco-friendly and biocompatible stabilizing agent is a thrust research domain. In this research work, application of dialdehyde cellulose (DAC) was studied to understand the effect on the enzymatic and conformational stability in collagen. The secondary structure of collagen is not significantly altered on interaction with DAC. But, it was found that DAC lead to changes in the amplitude of the circular dichroic (CD) spectrum but did not alter the triple helical conformation of collagen. DAC treated collagen exhibited 93% resistance to collagenolytic hydrolysis. Conversely, DAC treated collagenase exhibited 89% inhibition against collagen degradation and the inhibition was found to be concentration dependent. The kinetics of inhibition of collagenase by DAC was derived from the extent of hydrolysis of (2-furanacryloyl-L-leucyl-glycyl-L-prolyl-L-alanine), FALGPA. DAC exhibited non-competitive mode of inhibition against collagenase. CD data on DAC-modified collagenase substantiate the hypothesis that the inhibition of collagenase by DAC arises from secondary and quaternary structural changes in the enzyme. Gaining new insights in understanding the mechanism of stabilization of collagen by DAC through kinetics of inhibition of collagenase was presented. Note de contenu : - MATERIALS AND METHODS : Materials - Methods - Preparation of DAC - Preparation of crosslinked collagen - Resistance to collagenase - Inhibition of collagenase activity - Kinetic investigation - Inhibition of collagenase by DAC - Conformational changes of DAC stabilized collagen - RESULTS AND DISCUSSION : Inhibition of collagenase - DAC treated collagenase resistance of native collagen - Conformational changes in DAC stabilized collagen - Conformational changes in DAC treated collagenase - Kinetic analysis of inhibition of collagenase by DAC - Mechanism of inhibition of collagenase by DAC En ligne : https://drive.google.com/file/d/1SE-oSDIEYjm4_Qrm6DaXeblWS7zipi-Z/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=23452 [article]

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