Molecular and structural insights into skin collagen reveals several factors that influence its architecture

Naffa, Rafea; Maidment, Catherine; Ahn, Meekyung; Ingham, Bridget; Hinkley, Simon F.R.; Norris, Gillian E.

doi:10.1016/j.ijbiomac.2019.01.151

Cited by 30 publications

(27 citation statements)

References 75 publications

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“…Sample preparation is relatively simple as compared to other analytical techniques, such as high-performance liquid chromatography (HPLC) and colorimetric methods [18][19][20][21][22]. Finding the variations in the initial leather processing steps reduces the costs of down-stream processing.…”

Section: Introductionmentioning

confidence: 99%

Raman and Atr-Ftir Spectroscopy Towards Classification of Wet Blue Bovine Leather Using Ratiometric and Chemometric Analysis

et al. 2020

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There is a substantial loss of value in bovine leather every year due to a leather quality defect known as "looseness". Data show that 7% of domestic hide production is affected to some degree, with a loss of $35 m in export returns. This investigation is devoted to gaining a better understanding of tight and loose wet blue leather based on vibrational spectroscopy observations of its structural variations caused by physical and chemical changes that also affect the tensile and tear strength. Several regions from the wet blue leather were selected for analysis. Samples of wet blue bovine leather were collected and studied in the sliced form using Raman spectroscopy (using 532 nm excitation laser) and Attenuated Total Reflectance-Fourier Transform InfraRed (ATR-FTIR) spectroscopy. The purpose of this study was to use ATR-FTIR and Raman spectra to classify distal axilla (DA) and official sampling position (OSP) leather samples and then employ univariate or multivariate analysis or both. For univariate analysis, the 1448 cm − 1 (CH 2 deformation) band and the 1669 cm − 1 (Amide I) band were used for evaluating the lipid-to-protein ratio from OSP and DA Raman and IR spectra as indicators of leather quality. Curve-fitting by the sums-of-Gaussians method was used to calculate the peak area ratios of 1448 and 1669 cm − 1 band. The ratio values obtained for DA and OSP are 0.57 ± 0.099, 0.73 ± 0.063 for Raman and 0.40 ± 0.06 and 0.50 ± 0.09 for ATR-FTIR. The results provide significant insight into how these regions can be classified. Further, to identify the spectral changes in the secondary structures of collagen, the Amide I region (1600-1700 cm − 1) was investigated and curve-fitted-area ratios were calculated. The 1648:1681 cm − 1 (non-reducing: reducing collagen types) band area ratios were used for Raman and 1632:1650 cm − 1 (triple helix: α-like helix collagen) for IR. The ratios show a significant difference between the two classes. To support this qualitative analysis, logistic regression was performed on the univariate data to classify the samples quantitatively into one of the two groups. Accuracy for Raman data was 90% and for ATR-FTIR data 100%. Both Raman and ATR-FTIR complemented each other very well in differentiating the two groups. As a comparison, and to reconfirm the classification, multivariate analysis was performed using Principal Component Analysis (PCA) and Linear Discriminant Analysis (LDA). The results obtained indicate good classification between the two leather groups based on protein and lipid content. Principal component score 2 (PC2) distinguishes OSP and DA by symmetrically grouping samples at positive and negative extremes. The study demonstrates an excellent model for wider research on vibrational spectroscopy for early and rapid diagnosis of leather quality.

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Section: Introductionmentioning

confidence: 99%

Raman and Atr-Ftir Spectroscopy Towards Classification of Wet Blue Bovine Leather Using Ratiometric and Chemometric Analysis

et al. 2020

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“…During chrome tanning, the carboxylate (−COO − ) groups of aspartic (Asp) and glutamic (Glu) acid residues of collagen are bonded covalently [7], causing significant structural changes in collagen [40,41]. Similarly, the removal of structure stabilizing natural crosslinks can also cause changes in the collagen structure [3,42]. The interaction between natural and artificial crosslinks can therefore be studied by analysing the structural changes of collagen.…”

Section: Quantification Of Natural Crosslinks In Skin Collagen: Relatmentioning

confidence: 99%

“…Collagen type I is the main component of many loadbearing tissues including skin, bone, tendons, ligaments and dentin in teeth [1]. The biomechanical strength of tissue depends on the organisation of collagen molecules in the fibrils and fibres, which is controlled by the types and amount of proteoglycans and stabilised by covalent crosslinks [2,3]. Covalent crosslinks are formed between two or three collagen molecules during the fibrillogenesis step of the biosynthesis of collagen [2].…”

Section: Introductionmentioning

confidence: 99%

“…Several types of naturally-occurring covalent crosslinks have been identified in different collagenous materials, including dehydrodihydroxylysinonorleucine (deH-DHLNL), deoxypyridinoline (DPyr), pyridinoline (Pyr), dehydrohydroxylysinonorleucine (deH-HLNL), histidinohydroxylysinonorleucine (HHL) and histidinohydroxymerodesmosine (HHMD), in which deH-HLNL, HHL and HHMD are the major crosslinks in the collagen from skins and hides [2][3][4]. These crosslinks can be classified as reducible and non-reducible [2].…”

Section: Introductionmentioning

confidence: 99%

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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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“…To date, five types of crosslinks have been identified in bovine skins (Avery & Bailey, 2008;Naffa et al, 2016), i.e. divalent dehydro-hydroxylysinonorleucine (deH-HLNL) and dehydro-dihydroxylysinonorleucine (deH-DHLNL), trivalent crosslinked pyridinoline (Pyr) and histidinohydroxylysinonorleucine (HHL), and tetravalent crosslinked dehydro-histidinohydroxymerodesmosine (deH-HHMD), although its presence in vivo is disputed (Naffa et al, 2019;Avery & Bailey, 2008). However, amongst these five crosslinks, deH-HLNL, deH-DHLNL and deH-HHMD contain a C N bond and are labile to acidic conditions (Avery & Bailey, 2008).…”

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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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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Molecular and structural insights into skin collagen reveals several factors that influence its architecture

Cited by 30 publications

References 75 publications

Raman and Atr-Ftir Spectroscopy Towards Classification of Wet Blue Bovine Leather Using Ratiometric and Chemometric Analysis

Raman and Atr-Ftir Spectroscopy Towards Classification of Wet Blue Bovine Leather Using Ratiometric and Chemometric Analysis

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

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

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