Comparison of liquid chromatography with fluorescence detection to liquid chromatography-mass spectrometry for amino acid analysis with derivatisation by 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate: Applications for analysis of amino acids in skin

Naffa, Rafea; Holmes, Geoff; Zhang, Wenkai; Maidment, Catherine; Shehadi, Ihsan A.; Norris, Gillian E.

doi:10.1016/j.arabjc.2019.05.002

Cited by 17 publications

(8 citation statements)

References 37 publications

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“…To quantify Tryptophan, the column Xbridge (150 mm × 4.6 mm × 5 µm) (Water, Milford, MA, USA) and mobile phase using H 2 O:acetonitrile (v/v: 95:5) with isocratic elution were used. The excited wavelength and emission wavelength were λex = 295 nm and λem = 345 nm, respectively [31].…”

Section: Characterization and Analytical Methodsmentioning

confidence: 99%

Adsorptive Removal of Antibiotic Ciprofloxacin from Aqueous Solution Using Protein-Modified Nanosilica

Pham

Nguyen

et al. 2020

Polymers

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The present study aims to investigate adsorptive removal of molecular ciprofloxacin using protein-modified nanosilica (ProMNS). Protein was successfully extracted from Moringa seeds while nanosilica was synthesized from rice husk. Fourier-transform infrared (FTIR), ultraviolet visible (UV-Vis) and high-performance liquid chromatography (HPLC) were used to evaluate the characterization of protein. Adsorption of protein onto nanosilica at different pH and ionic strength was thoroughly studied to modify nanosilica surface. The removal efficiency of antibiotic ciprofloxacin (CFX) increased from 56.84% to 89.86% after surface modification with protein. Effective conditions for CFX removal using ProMNS were systematically optimized and found to be pH 7.0, adsorption time 90 min, adsorbent dosage 10 mg/mL, and ionic strength 1 mM KCl. A two-step model was successfully used to fit the adsorption isotherms of CFX onto ProMNS at different ionic strength while a pseudo-second-order model could fit adsorption kinetic of CFX onto ProMNS very well. Maximum adsorption capacity was very high that reached to 85 mg/g. Adsorption of CFX onto ProMNS decreased with increasing KCl concentration, suggesting that adsorption of CFX onto ProMNS is mainly controlled by electrostatic attraction between positively charged ProMNS surface and anionic species of CFX. Adsorption mechanisms of CFX onto ProMNS were discussed in detail based on adsorption isotherms, the change in surface charge by zeta potentail and the change in functional groups by FT-IR. The removal of CFX after three regenerations was greater than 73% while CFX removal from an actual hospital wastewater using ProMNS reached to 70%. Our results suggest that ProMNS is a new and eco-friendly adsorbent to remove antibiotics from aqueous solutions.

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Section: Characterization and Analytical Methodsmentioning

confidence: 99%

Adsorptive Removal of Antibiotic Ciprofloxacin from Aqueous Solution Using Protein-Modified Nanosilica

Pham

Nguyen

et al. 2020

Polymers

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“…In summary, a 100 mg of sample was placed in 4.0 mL of 6.0 M of HCl then heated at 105 • C for 24 h. The acid was then removed by SpeedVac (Savant™ SPD131DDA, ThermoFisher) and dissolved in 2.0 mL of water. Ten microliters was removed from each sample and diluted to 1.0 mL with water for hydroxyproline analysis [41]. The solution was injected into Cogent Diamond Hydride column then eluted using isocratic and gradient conditions for biological product samples and gelatin films, respectively.…”

Section: Preparation Of Samplesmentioning

confidence: 99%

Rapid and simultaneous analysis of advanced glycation end products on silica hydride column: Comparison of ultraviolet, fluorescence, and mass spectrometry detectors

Naffa

Gaar

Zhang

et al. 2020

Separation Science Plus

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Glycation of collagen produces advanced glycation end products including pentosidine, glyoxal-lysine dimer, and methylglyoxal-lysine dimer. These products are markers for aging and associated with the development of several diseases. In this study, a rapid and simultaneous analytical method for pentosidine, glyoxallysine dimer, and methylglyoxal-lysine dimer was developed. The separation of advanced glycation end products was carried out on a silica hydride column using either acetonitrile or methanol in water with 0.1% (v/v) formic acid. A total run time of <5.5 min was achieved using isocratic elution and 11 min using gradient conditions. The gradient elution also allowed the rapid and simultaneous of collagen crosslinks and advanced glycation end products in one run. The eluted peaks were detected by mass spectrometry then the fragmentation was measured by tandem mass spectrometry to confirm their identity. The method developed herein was successfully applied to high-performance liquid chromatography with fluorescence and ultraviolet detection. Although the ultraviolet detection sensitivity of glyoxal-lysine and methylglyoxal-lysine dimers is low, it is useful for preparative work for the collection of intact advanced glycation end-products. This method was applied to several biological sample products and used to monitor the formation of glycation product in gelatin treated with glucose.

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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 total ion chromatograms (TIC) produced were examined and quantitation was carried out using Thermo Xcalibur 3.0 software (Thermo Fisher Scientific, San Jose, USA). Hydroxylysinonorleucine (HLNL), histidinohydroxylysinonorleucine (HHL) and histidinohydroxymerodesmosine (HHMD) concentrations were determined then normalized to the collagen content of the sample which was calculated based on their hydroxyproline content [27][28][29].…”

Section: Analysis Of Collagen Crosslinks By Liquidchromatography Highmentioning

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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Comparison of liquid chromatography with fluorescence detection to liquid chromatography-mass spectrometry for amino acid analysis with derivatisation by 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate: Applications for analysis of amino acids in skin

Cited by 17 publications

References 37 publications

Adsorptive Removal of Antibiotic Ciprofloxacin from Aqueous Solution Using Protein-Modified Nanosilica

Adsorptive Removal of Antibiotic Ciprofloxacin from Aqueous Solution Using Protein-Modified Nanosilica

Rapid and simultaneous analysis of advanced glycation end products on silica hydride column: Comparison of ultraviolet, fluorescence, and mass spectrometry detectors

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

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