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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Molecular level understanding of the stability difference in collagen induced by chromium sulfate and aluminum sulfate / Weimo Han in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 101, N° 6 (11-12/2017)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 101, N° 6 (11-12/2017) . - p. 273-279 Titre : Molecular level understanding of the stability difference in collagen induced by chromium sulfate and aluminum sulfate Type de document : texte imprimé Auteurs : Weimo Han, Auteur ; Jianfei Zhou, Auteur ; Wenhua Zhang, Auteur ; Bi Shi, Auteur Année de publication : 2017 Article en page(s) : p. 273-279 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène -- Stabilité Sulfate d'aluminium Sulfate de chrome Tannage minéral Tannage dans lequel interviennent différents minéraux. Le plus répandu est le tannage aux sels de chrome, mais aussi à l’aluminium Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Though the tanning process of both chromium(III) and aluminum(III) are mainly the reactions of coordination with the collagen side chain carboxyl groups, the stability toward water and denaturing temperature of Cr(III)-tanned leather is much higher than that of Al(III)-tanned leather. In this paper, the differences between Cr(III) and AI(III) tanning mechanisms are explored from the species distribution of tanning liquors and the thermodynamics of coordination reaction. First, there are more multinuclear metal species in Cr(III) tanning liquor than in Al(III) tanning liquor through visual Minteq. For example, at pH4 Cr3(OH)4(H2O)10 5+ accounted for 39% in 0.05mol/L Cr2(SO4)3, and Al (OH)4(H2O), only 0.04% in 0.05mol/L AI2(SO4)3. In addition, a large amount of negative species Al(SO4)2(H2O)2 (always about 30% in AI2(SO4)3) appeared in Al(III) tanning liquor, which would show low coordinating effect because of the electrostatic repulsion with the ionised collagen sidechain carboxyl groups. The density functional method (DFT) was used to study the kinetics (the electrophilic indexes w) and thermodynamics (the Gibbs energy change ?rG) of tanning reaction with Lanl2dz for metal atoms and 6-31g(d) for non-metal atoms. The results showed that the reactivity of multinuclear species is higher and the complexes formed by collagen and multinucIear species are more stable for both Cr(III) and Al(III), and the differences of ?rG between corresponding Cr(Ill) and Al(lll) tanning reactions are miner. Then the main reason for the lower shrinkage temperature of Al2(SO4)3 may be the lower contents of multinuclear aluminum species and the higher content of the negative specie Al(SO4)2(H2O)2 in AI(III) tanning liquor. These results suggested that appropriate masking agents which could increase the multinuclear aluminum species content and decrease the negative species content should improve the AI(III) tanning process Note de contenu : - METHODS : The main chromium and aluminum species present under the pH range of tanning - The models of collagen sidechain carboxyl groups - The theoretical parameters - RESULTS AND DISCUSSION : The main species in Cr(III) and Al(III) tanning liquor - The reactivity of chromium and aluminium species - The driving force of typical reaction of Cr(III) and Al(III) tanning En ligne : https://drive.google.com/file/d/1T7KdyR561R35KhADfXa1mw77cSrGZhXU/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=29658 [article]

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On the shrinkage kinetic of collagen / Guillermo O. Sarli in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 60, N° 4 (07-08/1976)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 60, N° 4 (07-08/1976) . - p. 113-117 Titre : On the shrinkage kinetic of collagen Type de document : texte imprimé Auteurs : Guillermo O. Sarli, Auteur ; J. Raul Grigera, Auteur Année de publication : 1976 Article en page(s) : p. 113-117 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène -- Stabilité Température de retrait Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : The shrinkage kinetic of collagen was first used by Weiri to measure the activation enthalpy and entropy of the fibre-random coil transition of collagen. The early results shown a relative simple kinetic, characterised by a single parameter, namely the half time of the process. Later on, a more sophisticated inter-pretation of the kinetic was suggested. The curves shown in these works are very simple. The stability of collagen fibres is widely measured by means of the shrinkage temperature. This parameter is very easy to measure and, if the process is as simple as was described, it may well characterise the transition with enough accuracy. It is probable that on this account there have not been many new works published on shrinkage kinetic. However, by using a more refined measuring method to follow the shrinkage kinetic, we can show that the denaturation of collagen fibres is a process too complex to be characterised by the shrinkage temperature. The present note is intended to give some details of the measuring technique. Note de contenu : - Fig. 1 : Diagram of the apparatus - Fig. 2(a) : Shrinkage kinetic of rat tail tendon hydrated 24h in bidistilled water. (a) Shrunk in water - Fig. 2(b) : Shrunk in aqueous solution of dioxane 4.100 molal. En ligne : https://drive.google.com/file/d/1NBQSXEFcgv_cWRfShkCnoB3elCrpObb0/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=34116 [article]

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Stabilization of collagen by cross-linking with a ferrous-gluconic acid compound / Yang Mao in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 99, N° 2 (03-04/2015)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 99, N° 2 (03-04/2015) . - p. 91-94 Titre : Stabilization of collagen by cross-linking with a ferrous-gluconic acid compound Type de document : texte imprimé Auteurs : Yang Mao, Auteur ; Meng Yang, Auteur ; Shan Zhihua, Auteur ; Hongliang Zhu, Auteur ; Chen Hui, Auteur Année de publication : 2015 Article en page(s) : p. 91-94 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène -- Stabilité Gluconique, Acide L'acide gluconique (C6H12O7) est un acide très répandu aussi bien chez les animaux que dans les plantes. Il est le plus souvent intégré dans une molécule plus grande comme c'est le cas dans diverses gommes. Il est obtenu à partir de la gomme d'acacia, à partir de laquelle on l'isole sous la forme de cristaux en aiguilles fondant à 165 °C. Il est soluble dans l'eau et l'alcool. Il est autorisé en Europe comme additif alimentaire (E5748). Réticulation (polymérisation) Stabilité thermique Sulfate de fer Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : The stabilization of type I collagen is important to applications of collagen protein. In this paper, the stabilization of type I collagen with Fe-gluconic acid has been studied by various methods such as UV-vis and IR spectra, CD and DSC etc. Gluconic acid can form a compound with ferrous sulphate which can improve the thermal stability of type I collagen to an extent greater than that of Fe atone. The reaction molar ratio was 1:3 between Fe and gluconic acid. The increase of thermal stability is owed to cross-link formation between the compound and collagen. Note de contenu : - MATERIALS AND METHODS : Materiasl - Preparation of the ferrous-gluconic acid compound - UV-Vis spectra - FT-IR spectra - Elemental analysis - Viscosity measurements - Circular dichroism spectropolarimetry - Differential scanning calorimetry (DSC) - RESULTS AND DISCUSSION : UV-vis spectral studies - IR studies - Elemental analysis - Viscosity analysis of collagen-Fe-gluconic acid system - CD studies - DSC studies En ligne : https://drive.google.com/file/d/1c2YGlN8nKFP1Sllk9rvbveFNHT5ENQiM/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=23745 [article]

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Studies on further structural stabilisation of the chrome-collagen compound / T. Ramaswamy in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 59 (Année 1975)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 59 (Année 1975) . - p. 149-153 Titre : Studies on further structural stabilisation of the chrome-collagen compound Type de document : texte imprimé Auteurs : T. Ramaswamy, Auteur ; D. Ramaswamy, Auteur Année de publication : 1975 Article en page(s) : p. 149-153 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène -- Stabilité Complexes métalliques Résistance à la transpiration Résistance thermique Stabilité chimique Tannage au chrome Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : The factors causing detannage and stripping of chrome from chrome tanned collagen in the presence of sweat and heat have been outlined. Different methods of further stabilisation of the chrome-collagen compound have been discussed. Stabilisation through ligands which can form Mannich-type linkages has been assessed for heat and sweat resistance, and evidence for the participation of e-lysine groups of collagen in stabilisation has been obtained. Note de contenu : - EXPERIMENTAL : Complex formation with Cr3+ and dinuclear Cr2(OH)24+ species - RESULTS AND DISCUSSION : Role of protein groups in the stabilisation of chrome collagen complex En ligne : https://drive.google.com/file/d/1RCABT6nNjmbirYgewOWVu1285zeG-ljI/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=31837 [article]

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Studies on further structural stabilisation of the chrome-collagen compound / T. Ramaswamy in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 59, N° 5 (09-10/1975)  

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