A guide to high-efficiency chromium (III)-collagen cross-linking: Synchrotron SAXS and DSC study

Zhang, Yi; Snow, Tim; Smith, Andrew J.; Holmes, Geoff; Prabakar, Sujay

doi:10.1016/j.ijbiomac.2018.12.187

Cited by 30 publications

(26 citation statements)

References 34 publications

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“…Interestingly, this is contrary to previous reports on chrome tanned hides and skins, where an increase in D-periodicity is observed [14,18,19]. This anomaly is ambiguous but we speculate that the discrepancy of D-period changes after chrome tanning emanates from the differences in the intrinsic collagen structure of the hides and skins [13,19]. The detailed mechanism of collagen D-period changes remains unclear, however, changes in D-period during chrome tanning can be attributed to the reaction of Cr species with telopeptidyl aspartic and glutamic acid residues that disturb the gap/overlap region of collagen [18].…”

Section: Saxs Peak Changes With Tanningcontrasting

confidence: 99%

“…1). Interestingly, this is contrary to previous reports on chrome tanned hides and skins, where an increase in D-periodicity is observed [14,18,19]. This anomaly is ambiguous but we speculate that the discrepancy of D-period changes after chrome tanning emanates from the differences in the intrinsic collagen structure of the hides and skins [13,19].…”

Section: Saxs Peak Changes With Tanningcontrasting

confidence: 95%

“…Collagen molecules are aligned in a quarter stagger structure, resulting in repeating gap/overlap regions within the fibrils [12,13]. Because of its ordered arrangement, molecular level information can be acquired by Xray scattering techniques, including diffraction, to measure the periodicity of the gap/overlap regions (D-period) and the size of collagen fibrils [14][15][16][17][18][19]. The interactions between water and collagen play a crucial role in the stability of the triple helix [20][21][22].…”

Section: Introductionmentioning

confidence: 99%

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Collagen structure changes during chrome tanning in propylene carbonate

et al. 2019

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Green solvents, such as propylene carbonate (PC), can be used in leather processing to improve the efficiency of chrome tanning and reduce wastewater. Here we report a combined small-angle X-ray scattering (SAXS) and differential scanning calorimetry (DSC) study on PC and its efficacy as a carrier medium during chrome tanning. SAXS analysis on the collagen structure of chrome tanned leather using PC, compared to conventionally tanned leather using water, showed an increase in Cr uptake in addition to the more uniform penetration of Cr through the leather cross-section. The increased binding of Cr to the collagen matrix drives the decreased hydration environment of the collagen triple helix. Furthermore, DSC studies show a uniform hydrothermal stability for the PC samples due to the more even distribution of Cr through the collagen matrix. Understanding the mechanisms by which chrome tanning occurs in non-aqueous solvents can guide us towards a more sustainable future for the leather industry.

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Section: Saxs Peak Changes With Tanningcontrasting

confidence: 99%

Section: Saxs Peak Changes With Tanningcontrasting

confidence: 95%

Section: Introductionmentioning

confidence: 99%

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Collagen structure changes during chrome tanning in propylene carbonate

et al. 2019

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“…: II, 185 • C; III, 200 • C; and IV, 152 • C. Collagen materials exposed to high temperatures endure irreversible denaturation process [81][82][83][84][85][86]. Previous thermo-analytical studies of denaturation of collagen report that the denaturation temperature for bovine skin is 55 • C [87], bovine intramuscular connective tissue 90 • C [88], rat tail collagen 65 • C [89], bovine skin 50-55 • C [84], and type I collagen from bovine skin soluble in acid 117 • C [90]. As the water content is higher, collagen denaturation temperature gets higher, and this phenomenon may be observed in this study.…”

Section: Differential Scanning Calorimetry (Dsc)mentioning

confidence: 99%

Bovine Decellularized Amniotic Membrane: Extracellular Matrix as Scaffold for Mammalian Skin

et al. 2020

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Decellularized membranes (DM) were obtained from bovine amniotic membranes (BAM) using four different decellularization protocols, based on physical, chemical, and mechanical treatment. The new material was used as a biological scaffold for in vitro skin cell culture. The DM were characterized using hematoxylin-eosin assay, scanning electron microscopy (SEM), Fourier transform infrared spectroscopy (FTIR-ATR), and differential scanning calorimetry (DSC). The in vitro cytotoxicity of DM was evaluated using MTT. The efficacy of decellularization process was assessed through DNA quantification and electrophoresis. All the used protocols showed a high effectiveness in terms of elimination of native cells, confirmed by DNA extraction and quantification, electrophoresis, and SEM, although protocol IV removes the cellular contents and preserve the native extracellular matrix (ECM) architecture which it can be considered as the most effective in terms of decellularization. FTIR-ATR and DSC on the other hand, revealed the effects of decellularization on the biochemical composition of the matrices. There was no cytotoxicity and the biological matrices obtained were a source of collagen for recellularization. The matrices of protocols I, II, and III were degraded at day 21 of cell culture, forming a gel. The biocompatibility in vitro was demonstrated; hence these matrices may be deemed as potential scaffold for epithelial tissue regeneration.

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“…Theoretical molecular weight is calculated and presented below each molecule [34][35][36] macros [31] in the Igor software package (version 6.3.7.2, Wavemetrics, USA) adapted for the QUOKKA instrument. The reduced 1D data was analysed using an inhouse developed fitting software [32,33]. The relative diffraction peak intensities were calculated as R i/j = A i /A j , where A i and A j is the area of peak i and j.…”

Section: Small-angle Neutron Scattering (Sans)mentioning

confidence: 99%

Quantitative and structural analysis of isotopically labelled natural crosslinks in type I skin collagen using LC-HRMS and SANS

et al. 2019

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Collagen structure in biological tissues imparts its intrinsic physical properties by the formation of several covalent crosslinks. For the first time, two major crosslinks in the skin dihydroxylysinonorleucine (HLNL) and histidinohydroxymerodesmosine (HHMD), were isotopically labelled and then analysed by liquid-chromatography high-resolution accurate-mass mass spectrometry (LC-HRMS) and small-angle neutron scattering (SANS). The isotopic labelling followed by LC-HRMS confirmed the presence of one imino group in both HLNL and HHMD, making them more susceptible to degrade at low pH. The structural changes in collagen due to extreme changes in the pH and chrome tanning were highlighted by the SANS contrast variation between isotopic labelled and unlabelled crosslinks. This provided a better understanding of the interaction of natural crosslinks with the chromium sulphate in collagen suggesting that the development of a benign crosslinking method can help retain the intrinsic physical properties of the leather. This analytical method can also be applied to study artificial crosslinking in other collagenous tissues for biomedical applications.

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A guide to high-efficiency chromium (III)-collagen cross-linking: Synchrotron SAXS and DSC study

Cited by 30 publications

References 34 publications

Collagen structure changes during chrome tanning in propylene carbonate

Collagen structure changes during chrome tanning in propylene carbonate

Bovine Decellularized Amniotic Membrane: Extracellular Matrix as Scaffold for Mammalian Skin

Quantitative and structural analysis of isotopically labelled natural crosslinks in type I skin collagen using LC-HRMS and SANS

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