{"title":"Second-Order Derivation Fourier Transform Infrared Spectral Analysis of Regenerated Wool Keratin Structural Changes","authors":"Zhe Jiang, Wenjia Li, Yuxia Wang, Qiang Wang","doi":"10.1177/23305517211060778","DOIUrl":null,"url":null,"abstract":"Keratin is a natural biopolymer with excellent biocompatibility and biodegradability properties. It is widely used in biomaterial construction. The secondary structure of keratin is essential in its applications. This structure is associated with its regeneration. In this study, the structure of regenerated keratin from wool was analyzed using the amide I, II, and III bands from second-order derivation Fourier transform infrared spectroscopy. The results showed that the regenerated wool keratin retained its molecular backbone with the cleavage of disulfide bonds. The amide I and II bands indicated that the content ratio of α-helix to non-α-helix structure was less in the regenerated keratin than that of raw wool. The amide III band confirmed the contents of α-helix/β-sheet/β-turn/random coil for raw wool (35%/31%/22%/13%) and regenerated keratin (26%/35%/23%/15%).","PeriodicalId":6955,"journal":{"name":"AATCC Journal of Research","volume":"9 1","pages":"43 - 48"},"PeriodicalIF":0.6000,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"AATCC Journal of Research","FirstCategoryId":"88","ListUrlMain":"https://doi.org/10.1177/23305517211060778","RegionNum":4,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"MATERIALS SCIENCE, TEXTILES","Score":null,"Total":0}
引用次数: 2
Abstract
Keratin is a natural biopolymer with excellent biocompatibility and biodegradability properties. It is widely used in biomaterial construction. The secondary structure of keratin is essential in its applications. This structure is associated with its regeneration. In this study, the structure of regenerated keratin from wool was analyzed using the amide I, II, and III bands from second-order derivation Fourier transform infrared spectroscopy. The results showed that the regenerated wool keratin retained its molecular backbone with the cleavage of disulfide bonds. The amide I and II bands indicated that the content ratio of α-helix to non-α-helix structure was less in the regenerated keratin than that of raw wool. The amide III band confirmed the contents of α-helix/β-sheet/β-turn/random coil for raw wool (35%/31%/22%/13%) and regenerated keratin (26%/35%/23%/15%).
期刊介绍:
AATCC Journal of Research. This textile research journal has a broad scope: from advanced materials, fibers, and textile and polymer chemistry, to color science, apparel design, and sustainability.
Now indexed by Science Citation Index Extended (SCIE) and discoverable in the Clarivate Analytics Web of Science Core Collection! The Journal’s impact factor is available in Journal Citation Reports.