FTIR investigation of the secondary structure of type I collagen: New insight into the amide III band

Stani, Chiaramaria; Vaccari, Lisa; Mitri, Elisa; Birarda, Giovanni

doi:10.1016/j.saa.2019.118006

Cited by 174 publications

(117 citation statements)

References 25 publications

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“…The results of the PCA are in agreement with previous investigations that use FTIR spectra to provide additional insights on protein, in particular collagen, composition and structure 29 , 31 , 32 , 37 , 53 – 55 . Different collagen types can be identified/discriminated efficiently using absorbances from selected regions of the spectrum 27 .…”

Section: Discussionsupporting

confidence: 90%

“…The resulting solution was filtered (Ezee-filter™) and freeze-dried. Recent FTIR research on collagen type I 32 has shown that heating between 20 and 80 ºC affects the relative intensity of some of the amide I and amide III vibrations. The intensity reduction/enhancement was lower than 5% for most of the bands and much of the change occurred between 40 and 50 ºC, stabilizing thereafter.…”

Section: Methodsmentioning

confidence: 99%

“…Despite its potential, few studies have used spectroscopic techniques to determine collagen preservation in archaeological bone [21][22][23][24][25] . Fourier Transform Infrared (FTIR) spectroscopy has been regarded as a suitable method to explore the structure of collagen [26][27][28][29][30][31][32] , by relating FTIR absorption bands (of the amide I, II and III) to specific chemical bonds and secondary structural features (α-helix, β-sheets, β-turns and random coils), even in the most recent investigations 32 . But, as early as the mid-twentieth century, there was a fundamental change in the comprehension of the collagen structure led by X-ray diffraction investigations, which showed that the traditional model was incorrect and the polyproline II (PPII) model was introduced and backed by later investigations, becoming the accepted model 4,[33][34][35][36] .…”

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confidence: 99%

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Linking structural and compositional changes in archaeological human bone collagen: an FTIR-ATR approach

Cortizas

López-Costas

2020

Sci Rep

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Collagen is the main structural and most abundant protein in the human body, and it is routinely extracted and analysed in scientific archaeology. Its degree of preservation is, therefore, crucial and several approaches are used to determine it. Spectroscopic techniques provide a cost-effective, non-destructive method to investigate the molecular structure, especially when combined with multivariate statistics (chemometric approach). In this study, we used FTIR-ATR spectroscopy to characterise collagen extracted from skeletons recovered from necropoleis in NW Spain spanning from the Bronze Age to eighteenth century AD. Principal components analysis was performed on a selection of bands and structural equation models (SEM) were developed to relate the collagen quality indicators to collagen structural change. Four principal components represented: (i) Cp1, transformations of the backbone protein with a residual increase in proteoglycans; (ii) Cp2, protein transformations not accompanied by changes in proteoglycans abundance; (iii) Cp3, variations in aliphatic side chains and (iv) Cp4, absorption of the OH of carbohydrates and amide. Highly explanatory SEM models were obtained for the traditional collagen quality indicators (collagen yield, C, N, C:N), but no relationship was found between quality and δ13C and δ15N ratios. The observed decrease in C and N content and increase in C:N ratios is controlled by the degradation of protein backbone components and the relative preservation of carbon-rich compounds, proteoglycans and, to a lesser extent, aliphatic moieties. Our results suggest that FTIR-ATR is an ideal technique for collagen characterization/pre-screening for palaeodiet, mobility and radiocarbon research.

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Section: Discussionsupporting

confidence: 90%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Linking structural and compositional changes in archaeological human bone collagen: an FTIR-ATR approach

Cortizas

López-Costas

2020

Sci Rep

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“…Amide III band extending between 1175 and 1310 cm −1 is associated with C–N stretching, N–H bending vibrations, C–C stretching, and C–H bending vibrations. Amide II lies in the region of 1500 to 1600 cm −1 [ 56 ]. The exact positions of all corresponding amide bands, summarized in Table 2 , uncovers minor statistically insignificant deviations in positions among all spectra.…”

Section: Resultsmentioning

confidence: 99%

“…From all collagen amide regions, Amide I and Amide III bands corresponded with the secondary structure the most. Amide II reflected conformation changes as well, but it was far less conformation sensitive than the other two regions [ 56 ]. The vibration of the Amide I band is directly related to the backbone conformation and hydrogen bonding pattern [ 43 ].…”

Section: Resultsmentioning

confidence: 99%

Synergistic Effect of Chitosan and Selenium Nanoparticles on Biodegradation and Antibacterial Properties of Collagenous Scaffolds Designed for Infected Burn Wounds

et al. 2020

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A highly porous scaffold is a desirable outcome in the field of tissue engineering. The porous structure mediates water-retaining properties that ensure good nutrient transportation as well as creates a suitable environment for cells. In this study, porous antibacterial collagenous scaffolds containing chitosan and selenium nanoparticles (SeNPs) as antibacterial agents were studied. The addition of antibacterial agents increased the application potential of the material for infected and chronic wounds. The morphology, swelling, biodegradation, and antibacterial activity of collagen-based scaffolds were characterized systematically to investigate the overall impact of the antibacterial additives. The additives visibly influenced the morphology, water-retaining properties as well as the stability of the materials in the presence of collagenase enzymes. Even at concentrations as low as 5 ppm of SeNPs, modified polymeric scaffolds showed considerable inhibition activity towards Gram-positive bacterial strains such as Staphylococcus aureus and methicillin-resistant Staphylococcus aureus and Staphylococcus epidermidis in a dose-dependent manner.

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Biomimetic Structural Protein Based Magnetic Responsive Scaffold for Enhancing Bone Regeneration by Physical Stimulation on Intracellular Calcium Homeostasis

Liang,

Zou,

et al. 2023

Adv Healthcare Materials

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Bone matrix has distinct architecture and biochemistry which present a barrier on synthesizing bone‐mimetic regenerative scaffolds. To mimic the natural structures and components of bone, we prepared the biomimetic structural decellularized extracellular matrix (ECM)/regenerated silk fibroin (RSF) scaffolds incorporated with magnetic nanoparticles (MNP) using a facile synthetic methodology. The ECM/RSF/MNP scaffold is hierarchically organized and interconnected porous structure with silk fibroin twined on the collagen nanofibers, mimicking the bone minimum unit morphology. The scaffold demonstrated saturation magnetization due to the presence of MNP, along with good cytocompatibility. Moreover, the β‐sheet crystalline domain of RSF and the chelated magnetic nanoparticles could mimic the deposition of hydroxyapatite and enhance compressive modulus of the scaffold by approximately 20%. The results indicated that an external static magnetic field (SMF) with a magnetic responsive scaffold effectively promoted cell migration, osteogenic differentiation, neogenesis of endotheliocytes in vitro and new bone formation in a critical‐size femur defect rat model. RNA sequencing revealed that the molecular mechanisms underlying this osteogenic effect involve calsequestrin‐2‐mediated Ca2+ release from the endoplasmic reticulum to activate Ca2+/calmodulin/calmodulin‐dependent kinase II signaling axis. Collectively, bionic magnetic scaffolds with SMF stimulation provide a potent strategy for bone regeneration through internal structural cues, biochemical composition and external physical stimulation on intracellular Ca2+ homeostasis.This article is protected by copyright. All rights reserved

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FTIR investigation of the secondary structure of type I collagen: New insight into the amide III band

Cited by 174 publications

References 25 publications

Linking structural and compositional changes in archaeological human bone collagen: an FTIR-ATR approach

Linking structural and compositional changes in archaeological human bone collagen: an FTIR-ATR approach

Synergistic Effect of Chitosan and Selenium Nanoparticles on Biodegradation and Antibacterial Properties of Collagenous Scaffolds Designed for Infected Burn Wounds

Biomimetic Structural Protein Based Magnetic Responsive Scaffold for Enhancing Bone Regeneration by Physical Stimulation on Intracellular Calcium Homeostasis

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