Role of X‐ray Scattering Techniques in Understanding the Collagen Structure of Leather

Buchanan, Jenna K.; Zhang, Yi; Holmes, Geoff; Covington, Anthony D; Prabakar, Sujay

doi:10.1002/slct.201902908

Cited by 11 publications

(15 citation statements)

References 73 publications

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“…2(b)]. The increase in overall peak intensity confirmed the synthetic crosslinking effect by chromium sulfate, in agreement with previous reports (Buchanan et al, 2019). The intermolecular packing of collagen follows a quarter-staggered arrangement, resulting in a gap and overlap banding structure with a characteristic periodicity in the axial direction (D-period) (Petruska & Hodge, 1964).…”

Section: Effect Of Natural and Synthetic Crosslinks On Collagen Strucsupporting

confidence: 89%

“…However, it is essential to understand the interplay between natural and synthetic crosslinks and their contribution to the heat stability of collagen structure, which still remains unclear. Using synchrotron-based small-angle X-ray scattering (SAXS), changes in the collagen structure during crosslinking and denaturation can be monitored in situ (Buchanan et al, 2019). Also, liquid chromatography-mass spectrometry (LC-MS) can be used to quantify the natural crosslinks present in skin collagen (Naffa et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

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In situ structural studies during denaturation of natural and synthetically crosslinked collagen using synchrotron SAXS

Zhang¹,

Buchanan²,

Naffa³

et al. 2020

J Synchrotron Radiat

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Collagen is an important biomacromolecule, making up the majority of the extracellular matrix in animal tissues. Naturally occurring crosslinks in collagen stabilize its intermolecular structure in vivo, whereas chemical treatments for introducing synthetic crosslinks are often carried out ex vivo to improve the physical properties or heat stability of the collagen fibres for applications in biomaterials or leather production. Effective protection of intrinsic natural crosslinks as well as allowing them to contribute to collagen stability together with synthetic crosslinks can reduce the need for chemical treatments. However, the contribution of these natural crosslinks to the heat stability of collagen fibres, especially in the presence of synthetic crosslinks, is as yet unknown. Using synchrotron small-angle X-ray scattering, the in situ role of natural and synthetic crosslinks on the stabilization of the intermolecular structure of collagen in skins was studied. The results showed that, although natural crosslinks affected the denaturation temperature of collagen, they were largely weakened when crosslinked using chromium sulfate. The development of synergistic crosslinking chemistries could help retain the intrinsic chemical and physical properties of collagen-based biological materials.

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Section: Effect Of Natural and Synthetic Crosslinks On Collagen Strucsupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

In situ structural studies during denaturation of natural and synthetically crosslinked collagen using synchrotron SAXS

Zhang¹,

Buchanan²,

Naffa³

et al. 2020

J Synchrotron Radiat

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“…We found that a decrease in D -periodicity from 65.44 nm to around 65.2 nm occurred after cross-linking, indicating that the collagen molecules are drawn closer together by the inter-molecular and intra-fibril cross-linking of DCMC with its small size (Table ), allowing its penetration through the lateral and axial gaps of the collagen molecules in the fibrils . The peak positions and intensities obtained from the SAXS spectrum are known to be associated with the cross-linking and dehydration of collagen fibers . The relative intensity of the fifth to third order peak ( R 5/3 ) was related to the covalent cross-linking between the cross-linking agent and collagen .…”

Section: Resultsmentioning

confidence: 92%

“…39 The peak positions and intensities obtained from the SAXS spectrum are known to be associated with the cross-linking and dehydration of collagen fibers. 40 The relative intensity of the fifth to third order peak (R 5/3 ) was related to the covalent cross-linking between the cross-linking agent and collagen. 38 The relative intensity of the sixth to fifth order peak (R 6/5 ) represented the dehydration of collagen due to the displacement of water by the cross-linking agent through non-covalent interactions.…”

Section: Resultsmentioning

confidence: 99%

Effect of Dialdehyde Carboxymethyl Cellulose Cross-Linking on the Porous Structure of the Collagen Matrix

Zhang

Mansel

et al. 2022

Biomacromolecules

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Porous structures are essential for some collagen-based biomaterials and can be regulated by crosslinkers. Herein, dialdehyde carboxymethyl cellulose (DCMC) crosslinkers with similar size but different aldehyde group contents were prepared through periodate oxidation of sodium carboxymethyl cellulose with varying degrees of substitution (DS). They can penetrate into the hierarchy of fibril and form inter-molecular and intra-fibril cross-linking within the collagen matrix due to their nanoscale sizes and reactive aldehyde groups. The collagen matrices possessed higher porosity, significantly greater proportion of large pores (Φ > 10 μm), and shorter D-periodicity after cross-linking, showing greater potential for biomedical applications. In addition, the crosslinked collagen matrices showed satisfactory biocompatibility and biodegradation. The decreased DS of carboxymethyl cellulose, which led to the increased aldehyde content of corresponding DCMC, brought about an enhanced cross-linking degree, porosity, and proportion of large pores of the crosslinked collagen matrix. DCMC dosage of 6% was sufficient for cross-linking and pore formation. Excess DCMC would physically deposit in the matrix and decrease the porosity instead. Therefore, the desired pore properties of the collagen matrix could be obtained by regulating the structure of DCMC and thereby achieving the required functions of the biomaterial.

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“…44 Even though the general chemistry used in hide and skin processing is well-known, the structural changes at the level of the collagen fibrils is just starting to be revealed utilizing x-ray scattering techniques. [45][46][47] Herein we focused on the macroscopic effect of the composition of the soaking solutions on water sorption by horsehide and the correlations with the properties of corresponding final leather material.…”

Section: Water Absorption By Horsehidementioning

confidence: 99%

Regeneration of Raw Hide Water Balance by Electrochemically Activated Water

Danylkovych

Korotych

Романюк

2020

JALCA

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Improving the collagen structure, which was impacted by the curing process, increases the efficiency of all subsequent structural transformations during leather production and results in the formation of a high-quality leather material. Herein, we studied the process of soaking green-salted horsehides in electrochemically activated aqueous solutions and the properties of resulting chrome-tanned leather. It was found that the process of soaking horsehides can be effectively carried out using an electrochemically activated solution (ECAS) – a mixture of catholyte and anolyte at a volume ratio of 5 : 1. Using this soaking solution, sodium sulfide (an environmentally harmful reagent), sodium carbonate, and detergent can be completely excluded from the technological solution. The use of ECAS at the soaking stage effectively regenerates the water balance of horsehides while maintaining a stable pH during the soaking process and increases the efficacy of liming and all subsequent processes. Considering the prominent structural differences (density and thickness) between the front and shell of horsehide, the developed method, which utilize ECAS for soaking, allows the entire process to be carried out on uncut horse hides instead of processing two parts separately, which is normally required. The chrome-tanned leather produced by the developed method in semi-industrial conditions has elastic-plastic properties which are superior compared to the leather produced by current technology. The developed method also results in increasing the area yield by 2.5%. The resulting elastic leather can be used for manufacturing a variety of articles, including clothing, accessories, and footwear.

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Role of X‐ray Scattering Techniques in Understanding the Collagen Structure of Leather

Cited by 11 publications

References 73 publications

In situ structural studies during denaturation of natural and synthetically crosslinked collagen using synchrotron SAXS

In situ structural studies during denaturation of natural and synthetically crosslinked collagen using synchrotron SAXS

Effect of Dialdehyde Carboxymethyl Cellulose Cross-Linking on the Porous Structure of the Collagen Matrix

Regeneration of Raw Hide Water Balance by Electrochemically Activated Water

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