Effect of Disulfide Bonds in Human Hair Fibers on the Melting Behavior of Their Crystalline Structure

Osaki, Atsushi; Okada, Michiko; Yamamoto, Kazushi; Joko, Kyohei

doi:10.5107/sccj.43.86

Cited by 1 publication

(2 citation statements)

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“…As mentioned previously, HPDSC can be used to analyse hair keratin containing an excess of water in pressure‐resistant capsules. In this method, Δ H D is ascribed as the denaturation of the helix of keratins and its magnitude depends upon the amount and structural integrity of the helix segment in the IFs [24]. Additionally, it has been reported that T D reflects the cross‐linking density of IFAPs [24].…”

Section: Discussionmentioning

confidence: 99%

“…In this method, Δ H D is ascribed as the denaturation of the helix of keratins and its magnitude depends upon the amount and structural integrity of the helix segment in the IFs [24]. Additionally, it has been reported that T D reflects the cross‐linking density of IFAPs [24]. In the present study, the fact that Δ H D decreased with age (Table 2) could be due to a change in the amount and the structural integrity of the helical material in the IFs and is consistent with our results from the visualization of the secondary structure of hair protein using FT‐IR coupled MCR (Figure 5).…”

Section: Discussionmentioning

confidence: 99%

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Age‐related hair denaturation related to protein carbonyls

Fuse,

Morita,

Matsue

2023

Intern J of Cosmetic Sci

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ObjectiveHair ageing is accompanied by hair fibres becoming irregularly shaped causing them to stick out in irregular directions or have more curliness and being spread out. This is believed to be due to changes within the hair fibre structure which occur with ageing, and one of the causes of these changes could be an increase in the number of protein carbonyl groups present in the hair. The aim of this study is to investigate the internal denaturation of hair related to protein carbonyls in attempt to gain new insight into age‐related changes that occur in hair.MethodsThe degree of carbonylation of the hair structural protein as determined by fluorescent labelling and Western blotting analysis was used to investigate the primary structure of hair protein. The amount of helix, a common conformation in the secondary structure of proteins, in hair in groups of women with different ages was also analysed using infrared microscopy coupled with multivariate curve resolution (MCR). From the results of this, an image of the two‐dimensional distribution of the α‐helices was generated for the hair taken from each age group. Also, high‐pressure differential scanning calorimetry (HPDSC) of the hair in water was performed on the hair taken from each age group to determine the peak temperature of endothermic effect and the enthalpy of denaturation.ResultsWe found that the amino group content in hair proteins decreased and Type II keratin, one of the subunits of intermediate filament, was more carbonylated with age. The results of the MCR indicated eight separate components, including components of the secondary structure of proteins, such as α helices and β sheets. Two‐dimensional images of the hair cross‐sections revealed that the presence of α helices decreased with age. In addition, data from the HPDSC showed that the enthalpy associated with the denaturing temperature also significantly decreased with age.ConclusionThese results suggest that there is a negative correlation between age and structural integrity of the helix segment in intermediate filament. The results of this study also show that there is a positive correlation between age‐related hair denaturation and protein carbonyls.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%