Liquid chromatography-electrospray ionization mass spectrometry for the simultaneous quantitation of collagen and elastin crosslinks

Naffa, Rafea; Holmes, Geoff; Ahn, Meekyung; Harding, David; Norris, Gillian E.

doi:10.1016/j.chroma.2016.11.060

Cited by 31 publications

(39 citation statements)

References 39 publications

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“…Silica hydride is a unique stationary phase, which allows the use of both aqueous and nonpolar solvents to retain both hydrophobic and hydrophilic compounds . This type of column was used successfully for the separation of collagen crosslinks in skin including hydroxylysinonorleucine, dihydroxylysinonorleucine histidinohydroxylysinonorleucine, and histidinohydroxymerodesmosine . Initial results have been reported for the separation of PYR on a silica hydride column using water, acetonitrile, and methanol; however, a full study of both PYR and DPYR has not yet been completed .…”

Section: Introductionmentioning

confidence: 99%

Rapid analysis of pyridinoline and deoxypyridinoline in biological samples by liquid chromatography with mass spectrometry and a silica hydride column

Naffa

Watanabe

Zhang

et al. 2019

J of Separation Science

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Pyridinoline and deoxypyridinoline crosslinks are biomarkers found in urine for collagen degradation in bone turnover. For the first time, a rapid, sensitive, and ionpairing free method is described for the analysis of pyridinoline and deoxypyridinoline using ultra-high performance liquid chromatography with Cogent Diamond Hydride column and detection by Q Exactive hybrid quadrupole-orbitrap high resolution accurate mass spectrometry. The separation was achieved using both isocratic and gradient conditions and run time <5 min under isocratic conditions of 20% acetonitrile in water containing 0.1% formic acid. Pyridoxine was used as an internal standard and relative standard deviation of the retention times of both pyridinoline and deoxypyridinoline were <1%. The limit of detection was 0.082 ± 0.023 μM for pyridinoline and 0.118 ± 0.052 μM for deoxypyridinoline. The limit of quantitation was 0.245 ± 0.070 μM for pyridinoline and 0.354 ± 0.157 μM for deoxypyridinoline. The method was validated by the detection and quantitation of both pyridinoline and deoxypyridinoline in skin and urine samples. K E Y W O R D Sdeoxypyridinoline, mass spectrometry, pyridinoline, silica hydride column, urine analysis 1482

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Section: Introductionmentioning

confidence: 99%

Rapid analysis of pyridinoline and deoxypyridinoline in biological samples by liquid chromatography with mass spectrometry and a silica hydride column

Naffa

Watanabe

Zhang

et al. 2019

J of Separation Science

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“…Natural crosslinks in skin samples were analysed based on a previously published method by Naffa et al [6,27] Briefly, dry samples were weighed (20-40 mg) and rehydrated in a 1 mL of phosphate buffered saline (0.15 M sodium chloride, 0.05 M sodium phosphate pH 7.4). Control samples were analysed both as-prepared and stabilised (named as "stabilised control").…”

Section: Analysis Of Collagen Crosslinks By Liquidchromatography Highmentioning

confidence: 99%

“…The quantity of natural crosslinks was calculated from the integrated peak areas of the high-resolution mass spectra using our previously published protocols [6], and compared across each processing stages (Fig. 3).…”

Section: Quantification Of Natural Crosslinks In Skin Collagen: Relatmentioning

confidence: 99%

“…These crosslinks can be classified as reducible and non-reducible [2]. The reducible ones have aldimine bonds that are susceptible to acidic pH, which can be stabilised by reduction using sodium borohydride (NaBH 4 ) [5,6]. Depending on the applications, artificial crosslinkers are used to modify the mechanical properties and denaturation temperature of collagenous materials to meet with different purposes [2,7].…”

Section: Introductionmentioning

confidence: 99%

“…Several methods have been developed to analyse collagen crosslinks, including isotopic labelling [11,12], chromatography [4,6,13,14] and spectroscopy [15][16][17][18]. Although there are a large number of methods for crosslink analysis, only one method has been successfully applied for the characterisation and quantitative analysis of all known natural crosslinks in collagen using liquidchromatography coupled with high-resolution accuratemass mass spectrometry (LC-HRMS).…”

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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The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development

et al. 2018

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Collagen is the oldest and most abundant extracellular matrix protein that has found many applications in food, cosmetic, pharmaceutical, and biomedical industries. First, an overview of the family of collagens and their respective structures, conformation, and biosynthesis is provided. The advances and shortfalls of various collagen preparations (e.g., mammalian/marine extracted collagen, cell‐produced collagens, recombinant collagens, and collagen‐like peptides) and crosslinking technologies (e.g., chemical, physical, and biological) are then critically discussed. Subsequently, an array of structural, thermal, mechanical, biochemical, and biological assays is examined, which are developed to analyze and characterize collagenous structures. Lastly, a comprehensive review is provided on how advances in engineering, chemistry, and biology have enabled the development of bioactive, 3D structures (e.g., tissue grafts, biomaterials, cell‐assembled tissue equivalents) that closely imitate native supramolecular assemblies and have the capacity to deliver in a localized and sustained manner viable cell populations and/or bioactive/therapeutic molecules. Clearly, collagens have a long history in both evolution and biotechnology and continue to offer both challenges and exciting opportunities in regenerative medicine as nature's biomaterial of choice.

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Liquid chromatography-electrospray ionization mass spectrometry for the simultaneous quantitation of collagen and elastin crosslinks

Cited by 31 publications

References 39 publications

Rapid analysis of pyridinoline and deoxypyridinoline in biological samples by liquid chromatography with mass spectrometry and a silica hydride column

Rapid analysis of pyridinoline and deoxypyridinoline in biological samples by liquid chromatography with mass spectrometry and a silica hydride column

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

The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development

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