Characterization of Secondary Structure of Pig Hair Fiber Using Fourier-transform Infrared Spectroscopy

Mohan, N. H.; Choudhury, Minati; Ammayappan, L.; Pathak, P. K.; Chakraborty, Sujay; Thomas, R.; Debnath, Sanjoy; Paul, M. Saint; Sarma, D. K.

doi:10.1080/15440478.2020.1856272

Cited by 12 publications

(5 citation statements)

References 37 publications

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“…Utilizing prior references, we identified α-helix, β-sheets, β-turns, and disordered structural components and their individual microstructural components were depicted as fractions of the total area of the corresponding amide band (Figure B and Figure S3). , …”

Section: Resultsmentioning

confidence: 99%

“…Utilizing prior references, we identified α-helix, β-sheets, βturns, and disordered structural components and their individual microstructural components were depicted as fractions of the total area of the corresponding amide band (Figure 7B and Figure S3). 46,47 Within hair fibers, the prevalent hair keratin conformation is α-helix, 48 with approximately 40% of keratin in a β-sheet state according to another study. 49 The transformation between different keratin structures has a great influence on the mechanical properties of hair.…”

Section: Hair Repairing Mechanism Of Click Dyeingmentioning

confidence: 93%

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Multifunctional Hair Dyeing with Curcumin via Thiol-Michael Click Reaction

Wu,

Ma,

et al. 2024

ACS Appl. Eng. Mater.

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Plant-based colorants in hair dyeing are popular due to their lower toxicity for health and the environment compared to conventional chemically synthesized dyes. However, the application of plant colorants in hair dyeing is limited due to their low adsorption and poor fastness. In this study, we aimed to enhance the hair dyeing performance of a plant-based colorant (curcumin) by prelinking thiol groups (referred to as "click dyeing") and investigated the dyeing effect and restorative function. The results demonstrated that click dyeing significantly improved curcumin's coloring ability and color fastness, with the retention ratio of color reaching 80% after seven shampoo washes. Additionally, click dyeing enhanced the mechanical properties of the bleached hair and reduced keratin loss. Fluorescence labeling experiments confirmed that curcumin reacted with the introduced thiol groups through a thiol-Michael click reaction. After click dyeing, the mechanical properties of the hair fibers were repaired due to the formation of chemical bonds during the click reaction, resulting in a 9.81% increase in tensile strength compared to bleached hair before the hair dyeing process. The mechanism behind this enhancement lies in the restoration of the keratin conformation by click dyeing, bringing various properties back to their original state. Furthermore, the study verified curcumin's ability to resist photoaging through xenon arc lamp radiation and electron spin resonance (ESR) spectroscopy.

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Section: Resultsmentioning

confidence: 99%

Section: Hair Repairing Mechanism Of Click Dyeingmentioning

confidence: 93%

Multifunctional Hair Dyeing with Curcumin via Thiol-Michael Click Reaction

Wu,

Ma,

et al. 2024

ACS Appl. Eng. Mater.

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“…To further investigate the ability of 1,4‐n‐butylene dimaleate to restore the disrupted secondary conformation of reduced hair keratin, hair samples were analysed using FT‐IR spectroscopy (Figure 8a). The Amide I (1600–1700 cm −1 ) and Amide II (1500–1600 cm −1 ) regions were deconvoluted to resolve to identify individual secondary structural components of the hair fibre proteins [35]. Subtle differences in FT‐IR can be clearly observed after deconvolution (Figure 8b,c).…”

Section: Resultsmentioning

confidence: 99%

Reconnection of cysteine in reduced hair with alkylene dimaleates via thiol‐Michael click chemistry

Wu,

Ma,

Chen

et al. 2024

Intern J of Cosmetic Sci

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ObjectivesConventional hair permanent waving (PW) and permanent straightening processes typically involve two steps: reduction, for breaking ‐S‐S‐ bond in cystine into cysteine and oxidation for ‐S‐S‐ bond reconnection. However, it is known that the hair incurs damage during the oxidation step. In this work, we proposed a novel strategy to reconnect reduced disulfide bonds in hair via the thiol‐Michael click reaction, by using a symmetric Michael reagent.MethodsVirgin black Chinese hair was reduced using 8% wt thioglycolic acid and employed as model hair containing a high content of broken disulfide bonds. The reduced hair was treated with 1,4‐n‐butylene dimaleate. Raman spectroscopy and Fourier transform infrared spectroscopy (FT‐IR) were used to verify the chemical changes occurred in untreated and treated hair fibre. Single‐fibre mechanical properties and thermal properties of the hair were evaluated using tensile testing and differential scanning calorimetry (DSC), respectively.ResultsThe 1,4‐n‐butylene dimaleate could reconnect free thiol groups generated by disulfide bond reduction via thiol‐Michael click reaction and significantly improve the mechanical strength of hair compared to that of the reduced hair. Secondary conformational resolution analysis of FT‐IR results revealed that the content of α‐helix structure could be restored after treatment with 1,4‐n‐butylene dimaleate. The intermolecular forces established by the newly generated C‐S bonds compensate the broken disulfide bonds and enhance the fracture strength of the hair compared to that of reduced hair. Michael reagents of similar structure also showed similar performance in restoring the mechanical properties of reduced hair.ConclusionsOur data suggest that 1,4‐n‐butylene dimaleate can restore the mechanical properties of reduced hair by reconnecting reduced disulfide bonds and restoring the secondary conformation of hair keratin.

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“…The peak at 1153.00 cm −1 was shifted to 1260.78 cm −1 , corresponding to the amide III band. This band represents the stretching vibration of C-N and the bending vibration of N-H, which mainly arise from the combina-tion of -CH 2 in glycine with proline and calcium ions [55]. The peak at 625.33 cm −1 was shifted to 614.72 cm −1 , indicating the substitution of the N-H bond by N-Ca.…”

Section: Fourier Transform Infrared (Ftir) Spectroscopymentioning

confidence: 97%

“…Compared with that of WMPHs-COS, the wavenumber of WMPHs-COS-Ca shifted from 3378.82 cm −1 to 3362.42 cm −1 , which was attributed to the -NH stretching vibration corresponding to the Ca 2+ binding site, suggesting that N-H plays a role in chelate formation, possibly due to the dipole field effect or induction effect [54]. The vibrational spectral region at 1700-1500 cm −1 corresponds to the stretching vibration of the amide I band (1700-1600 cm −1 ; C=O) and the amide II band (1580-1510 cm −1 ; C-N,N-H) [55]. The peak at 1662.89 cm −1 shifted to 1658.07 cm −1 , indicating a change in the C=O absorption peak and suggesting that C=O is involved in the formation of WMPHs-COS-Ca, which aligns with the findings of Wu, He [27].…”

Section: Fourier Transform Infrared (Ftir) Spectroscopymentioning

confidence: 99%

Glycated Walnut Meal Peptide–Calcium Chelates: Preparation, Characterization, and Stability

Wang,

Zhao,

Yang

et al. 2024

Foods

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Finding stable and bioavailable calcium supplements is crucial for addressing calcium deficiency. In this study, glycated peptide–calcium chelates (WMPHs–COS–Ca) were prepared from walnut meal protein hydrolysates (WMPHs) and chitosan oligosaccharides (COSs) through the Maillard reaction, and the structural properties and stability of the WMPHs–COS–Ca were characterized. The results showed that WMPHs and COSs exhibited high binding affinities, with a glycation degree of 64.82%. After glycation, Asp, Lys, and Arg decreased by 2.07%, 0.46%, and 1.06%, respectively, which indicated that these three amino acids are involved in the Maillard reaction. In addition, compared with the WMPHs, the emulsifying ability and emulsion stability of the WMPHs–COS increased by 10.16 mg2/g and 52.73 min, respectively, suggesting that WMPHs–COS have better processing characteristics. After chelation with calcium ions, the calcium chelation rate of peptides with molecular weights less than 1 kDa was the highest (64.88%), and the optimized preparation conditions were 5:1 w/w for WMPH–COS/CaCl2s, with a temperature of 50 °C, a chelation time of 50 min, and a pH of 7.0. Scanning electron microscopy showed that the “bridging role” of WMPHs-COS changed to a loose structure. UV–vis spectroscopy and Fourier transform infrared spectrometry results indicated that the amino nitrogen atoms, carboxyl oxygen atoms, and carbon oxygen atoms in WMPHs-COS chelated with calcium ions, forming WMPHs-COS-Ca. Moreover, WMPHs-COS-Ca was relatively stable at high temperatures and under acidic and alkaline environmental and digestion conditions in the gastrointestinal tract, indicating that WMPHs–COS–Ca have a greater degree of bioavailability.

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Characterization of Secondary Structure of Pig Hair Fiber Using Fourier-transform Infrared Spectroscopy

Cited by 12 publications

References 37 publications

Multifunctional Hair Dyeing with Curcumin via Thiol-Michael Click Reaction

Multifunctional Hair Dyeing with Curcumin via Thiol-Michael Click Reaction

Reconnection of cysteine in reduced hair with alkylene dimaleates via thiol‐Michael click chemistry

Glycated Walnut Meal Peptide–Calcium Chelates: Preparation, Characterization, and Stability

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