DFT:B3LYP/3-21G theoretical insights on the confocal Raman experimental observations in skin dermis of healthy young, healthy elderly, and diabetic elderly women

Soto, Claudio A. Telléz; Pereira, Lucas Medeiros; Santos, Laurita dos; Rajasekaran, Ramu; Fávero, P. P.; Martin, Aírton Abrahão

doi:10.1117/1.jbo.21.12.125002

Cited by 4 publications

(2 citation statements)

References 26 publications

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“…9). These two peaks are related to the local conformation around hydroxyproline (876 cm −1 ) and proline (1445 cm −1 ; this peak indicates the absence of hydrogen bonding in X-PRO carbonyl groups) [29][30][31][32]. Hydroxyproline and proline play crucial roles in determining collagen stability [33] and permit the sharp twisting of the collagen triple helix [34].…”

Section: Plasma Changes the Local Conformation And Association Of Collagen Molecules Which Play Crucial Roles In Biofunctionalizationmentioning

confidence: 99%

Surface biofunctionalization with liquid-phase plasma treatment of collagen molecules

Tanaka

Kanemura

Okumura

et al. 2021

Preprint

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Surface functionalization is a key process in rendering various materials biocompatible. Whereas a number of techniques and technologies have been developed for the purpose of biofunctionalization, plasma treatment enables highly efficient surface modification. Extending plasma treatment to biomolecules in the liquid phase will control biofunctionalization via a simple process. However, interactions between plasma discharge and biomolecules or solvents are poorly understood, potentially leading to the technical limitation as to the utility of plasma treatment. In this study, we developed a technology for substrate biofunctionalization that does not require surface modification but involves direct treatment of a collagen molecules with liquid-phase plasma discharge. Biofunctionalization of collagen by plasma treatment comprises three processes that increase its reactivity with hydrophobic substrates: (1) charge-dependent changes in surface and interfacial properties of the collagen solution; (2) local conformational changes of the collagen molecules without their global structural alterations; and (3) induction of a micelle-like association formed by collagen molecules. We anticipate such plasma-induced functionalization of protein molecules to provide a versatile technique in the applications of biomaterials, including those related to pharmaceuticals and cosmetics.

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Section: Plasma Changes the Local Conformation And Association Of Collagen Molecules Which Play Crucial Roles In Biofunctionalizationmentioning

confidence: 99%

Surface biofunctionalization with liquid-phase plasma treatment of collagen molecules

Tanaka

Kanemura

Okumura

et al. 2021

Preprint

View full text Add to dashboard Cite

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“…(d,f) if exposed hair sides. References [ 56 , 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 , 75 , 76 , 77 , 78 , 79 , 80 , 81 , 82 , 83 , 84 , 85 , 86 , 87 , 88 , 89 , 90 , 91 , 92 , 93 , 94 , 95 , 96 , 97 , 98 , 99 , 100 , 101 , 102 , 103 , 104 , 105 , 106 , 107 , 108 , ...…”

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Spectral Features Differentiate Aging-Induced Changes in Parchment—A Combined Approach of UV/VIS, µ-ATR/FTIR and µ-Raman Spectroscopy with Multivariate Data Analysis

et al. 2023

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From the moment of production, artworks are constantly exposed to changing environmental factors potentially inducing degradation. Therefore, detailed knowledge of natural degradation phenomena is essential for proper damage assessment and preservation. With special focus on written cultural heritage, we present a study on the degradation of sheep parchment employing accelerated aging with light (295–3000 nm) for one month, 30/50/80% relative humidity (RH) and 50 ppm sulfur dioxide with 30/50/80%RH for one week. UV/VIS spectroscopy detected changes in the sample surface appearance, showing browning after light-aging and increased brightness after SO2-aging. Band deconvolution of ATR/FTIR and Raman spectra and factor analysis of mixed data (FAMD) revealed characteristic changes of the main parchment components. Spectral features for degradation-induced structural changes of collagen and lipids turned out to be different for the employed aging parameters. All aging conditions induced denaturation (of different degrees) indicated by changes in the secondary structure of collagen. Light treatment resulted in the most pronounced changes for collagen fibrils in addition to backbone cleavage and side chain oxidations. Additional increased disorder for lipids was observed. Despite shorter exposure times, SO2-aging led to a weakening of protein structures induced by transitions of stabilizing disulfide bonds and side chain oxidations.

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Assessing glycation‐mediated changes in human cortical bone with Raman spectroscopy

Ünal

Uppuganti

Leverant

et al. 2018

Journal of Biophotonics

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Establishing a non-destructive method for spatially assessing advanced glycation end-products (AGEs) is a potentially useful step toward investigating the mechanistic role of AGEs in bone quality. To test the hypothesis that the shape of the amide I in the Raman spectroscopy (RS) analysis of bone matrix changes upon AGE accumulation, we incubated paired cadaveric cortical bone in ribose or glucose solutions and in control solutions for 4 and 16 weeks, respectively, at 37°C. Acquiring 10 spectra per bone with a 20X objective and a 830 nm laser, RS was sensitive to AGE accumulation (confirmed by biochemical measurements of pentosidine and fluorescent AGEs). Hyp/Pro ratio increased upon glycation using either 0.1 M ribose, 0.5 M ribose or 0.5 M glucose. Glycation also decreased the amide I sub-peak ratios (cm ) 1668/1638 and 1668/1610 when directly calculated using either second derivative spectrum or local maxima of difference spectrum, though the processing method (eg, averaged spectrum vs individual spectra) to minimize noise influenced detection of differences for the ribose-incubated bones. Glycation however did not affect these sub-peak ratios including the matrix maturity ratio (1668/1690) when calculated using indirect sub-band fitting. The amide I sub-peak ratios likely reflected changes in the collagen I structure.

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DFT:B3LYP/3-21G theoretical insights on the confocal Raman experimental observations in skin dermis of healthy young, healthy elderly, and diabetic elderly women

Cited by 4 publications

References 26 publications

Surface biofunctionalization with liquid-phase plasma treatment of collagen molecules

Surface biofunctionalization with liquid-phase plasma treatment of collagen molecules

Spectral Features Differentiate Aging-Induced Changes in Parchment—A Combined Approach of UV/VIS, µ-ATR/FTIR and µ-Raman Spectroscopy with Multivariate Data Analysis

Assessing glycation‐mediated changes in human cortical bone with Raman spectroscopy

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