Age-related hair denaturation related to protein carbonyls

IF 2.7 4区医学 Q2 DERMATOLOGY International Journal of Cosmetic Science Pub Date : 2023-12-11 DOI:10.1111/ics.12934

Naoya Fuse, Shigeaki Morita, Yukako Matsue

{"title":"Age-related hair denaturation related to protein carbonyls","authors":"Naoya Fuse, Shigeaki Morita, Yukako Matsue","doi":"10.1111/ics.12934","DOIUrl":null,"url":null,"abstract":"<div>\n \n \n <section>\n \n <h3> Objective</h3>\n \n <p>Hair 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.</p>\n </section>\n \n <section>\n \n <h3> Methods</h3>\n \n <p>The 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.</p>\n </section>\n \n <section>\n \n <h3> Results</h3>\n \n <p>We 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.</p>\n </section>\n \n <section>\n \n <h3> Conclusion</h3>\n \n <p>These 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.</p>\n </section>\n </div>","PeriodicalId":13936,"journal":{"name":"International Journal of Cosmetic Science","volume":"46 3","pages":"348-356"},"PeriodicalIF":2.7000,"publicationDate":"2023-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Cosmetic Science","FirstCategoryId":"3","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/ics.12934","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"DERMATOLOGY","Score":null,"Total":0}

引用次数: 0

Abstract

Objective

Hair 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.

Methods

The 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.

Results

We 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.

Conclusion

These 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.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

与年龄有关的头发变性与蛋白质羰基有关

随着头发老化，头发纤维的形状变得不规则，导致它们向不规则的方向突出，或者变得更加卷曲和扩散。这被认为是由于随着年龄的增长，头发纤维结构发生了变化，而这些变化的原因之一可能是头发中蛋白质羰基数量的增加。本研究的目的是研究与蛋白质羰基相关的头发内部变性，试图获得与头发中发生的年龄相关变化的新见解。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

International Journal of Cosmetic Science DERMATOLOGY-

CiteScore

4.60

自引率

4.30%

发文量

期刊介绍： The Journal publishes original refereed papers, review papers and correspondence in the fields of cosmetic research. It is read by practising cosmetic scientists and dermatologists, as well as specialists in more diverse disciplines that are developing new products which contact the skin, hair, nails or mucous membranes. The aim of the Journal is to present current scientific research, both pure and applied, in: cosmetics, toiletries, perfumery and allied fields. Areas that are of particular interest include: studies in skin physiology and interactions with cosmetic ingredients, innovation in claim substantiation methods (in silico, in vitro, ex vivo, in vivo), human and in vitro safety testing of cosmetic ingredients and products, physical chemistry and technology of emulsion and dispersed systems, theory and application of surfactants, new developments in olfactive research, aerosol technology and selected aspects of analytical chemistry.