Unravelling the mechanism of the interactions of oxazolidine A and E with collagens in ovine skin

Choudhury, Santanu Deb; Dasgupta, Samir; Norris, Gillian E.

doi:10.1016/j.ijbiomac.2006.09.003

Cited by 29 publications

(15 citation statements)

References 22 publications

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“…20,21 Pre-tanning agents such as Zoldine ZE are commonly used to improve the penetration of main tanning agents through the collagen matrix in the skin, by decreasing the availability of amino acid side chain groups on the collagen molecule. When the samples were treated with the main tanning agents BCS, So-Si or So-Si + BCS (stage 3), different rates of xation were observed based on the colour of the oats and the cross-sections of the skins.…”

Section: -6mentioning

confidence: 99%

Can sodium silicates affect collagen structure during tanning? Insights from small angle X-ray scattering (SAXS) studies

et al. 2017

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The effect of sodium silicates on collagen structure during leather processing was investigated. Small angle X-ray scattering (SAXS) and differential scanning calorimetry (DSC) reveal that the molecular structure and thermal stabilities of the sodium silicate treated leathers (So-Si and So-Si + BCS) were different to the conventionally processed chromium treated leathers (BCS). The collagen fibrils were observed to be coated by aggregates of silica, which did not affect the axial periodicity (D-period) of the collagen molecules. However, an increase in collagen fibril diameter was observed during the main tanning step when sodium silicates were used. This could be due to the swelling of collagen fibers from the high alkaline conditions of sodium silicates. From DSC studies, it was also found that sodium silicate treated samples impart no effect on collagen stabilization in the absence of chromium(III). However, a pseudostabilization effect is observed in the So-Si + BCS samples, possibly due to the inability of the collagen molecules to undergo conformational changes due to the silica coating on the collagen fibrils.The tanning of leather involves chemically intense processes leading to environmental pollution, resulting in a demand for cleaner but effective collagen stabilization mechanisms for the leather industry.1,2 Basic chromium(III) sulphate is the most common mineral tanning agent and, is preferred industrially because of the high hydrothermal stability. It has excellent properties in addition to relative short times required to produce nished leathers.3 However, poor uptake of chromium salts leads to high chemical and biological oxygen demand, and toxicity concerns relating to hexavalent chromium(VI) exposure, have led researchers to seek more environmentally friendly alternatives. 4-6Mineral tanning agents such as chromium, zirconium, aluminium, titanium and iron can all stabilize collagen and impart varying degrees of hydrothermal stability.3,7 Synthetic tanning agents (syntans) and vegetable tanning agents from plant polyphenols along with aldehydic cross-linkers are also commonly used, but typically in conjunction with mineral tannages.8 Combination tannages however, with or without mineral tanning agents, can overcome the issues that single tanning systems have with hydrothermal stability.9,10 For example, Vitolo and co-workers observed an increase in chromium uptake when sodium silicate was used in combination with basic chromium sulphate.11 Whilst pre-tans can improve the penetration and even distribution of the main tanning agents in the collagen matrix, a co-stabilizing agent can increase the efficiency of chrome uptake by reducing the amount of chrome required.8 With this idea of combining a weak and strong tanning agent, further studies have been carried out by investigating combinations of a number of tanning options and their effect on collagen stabilization. 4,6,9,12 Soluble silicates such as sodium silicate belong to a group of compounds that contain varying compositions of an alkali met...

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Section: -6mentioning

confidence: 99%

Can sodium silicates affect collagen structure during tanning? Insights from small angle X-ray scattering (SAXS) studies

et al. 2017

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“…As noted above, peptide 3 containing tyrosine did not produce any detectable reaction product with oxazolidine E although previous work had shown that tyrosine residues in skin peptides were modified upon reaction with oxazolidines (43). This modification was not the result of a bridging interaction between oxazolidine tyrosine and another amino acid, but occurred because an imine, formed as a result of the interaction of oxazolidine with the primary amino side chain of lysine, was able to make a covalent bond with the side chain of tyrosine.…”

Section: Resultsmentioning

confidence: 79%

Effect of Oxazolidine E on Collagen Fibril Formation and Stabilization of the Collagen Matrix

Choudhury

Haverkamp

Dasgupta

et al. 2007

J. Agric. Food Chem.

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Oxazolidine E, an aldehydic cross-linking agent, is used to impart hydrothermal stability to collagen. The purpose of this study was to investigate the exact nature of oxazolidine E induced cross-links with collagen by using synthetic peptides having sequence homology with collagen type I. Tandem mass spectrometry revealed the formation of methylol and Schiff-base adducts upon reaction of oxazolidine E with the peptides. This was confirmed by allowing the reaction to proceed under reducing conditions using cyanoborohydride. Mass spectrometry (MS)-MS analysis clearly showed interaction of tryptophan and lysine residues with oxazolidine E and demonstrated that arginine could be cross-linked with glycine in the presence of oxazolidine E through the formation of a methylene bridge. Collagen fibrils regenerated from monomers in the presence and absence of oxazolidine E were studied using atomic force microscopy to investigate morphological alterations. Regenerated fibrils showing the typical 65 nm D-banding pattern were obtained from those formed both in the presence and absence of oxazolidine E, and there was no evidence of a change in the D-periodicity of these fibrils. This indicated that oxazolidine E does not hinder collagen molecules from correctly aligning to form the quarter-stagger structure.

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“…The CD spectral changes with small deviations in Rpn ratio were thought to be the result of the aggregation of the crosslinked collagen molecules. Besides, Choudhury et al [22] investigated the interactions between oxazolidine and collagen by CD. Results showed that the conformation of collagen became more random with the increase of oxazolidine concentration.…”

Section: Discussionmentioning

confidence: 99%

Interactions of collagen molecules in the presence of N-hydroxysuccinimide activated adipic acid (NHS-AA) as a crosslinking agent

Zhang

2011

International Journal of Biological Macromolecules

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Unravelling the mechanism of the interactions of oxazolidine A and E with collagens in ovine skin

Cited by 29 publications

References 22 publications

Can sodium silicates affect collagen structure during tanning? Insights from small angle X-ray scattering (SAXS) studies

Can sodium silicates affect collagen structure during tanning? Insights from small angle X-ray scattering (SAXS) studies

Effect of Oxazolidine E on Collagen Fibril Formation and Stabilization of the Collagen Matrix

Interactions of collagen molecules in the presence of N-hydroxysuccinimide activated adipic acid (NHS-AA) as a crosslinking agent

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