再生羊毛角蛋白结构变化的二阶导数傅立叶变换红外光谱分析

IF 0.6 4区工程技术 Q4 MATERIALS SCIENCE, TEXTILES

AATCC Journal of Research Pub Date : 2022-01-01 DOI:10.1177/23305517211060778

Zhe Jiang, Wenjia Li, Yuxia Wang, Qiang Wang

{"title":"再生羊毛角蛋白结构变化的二阶导数傅立叶变换红外光谱分析","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":null,"pages":null},"PeriodicalIF":0.6000,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":"{\"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\":null,\"pages\":null},\"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}","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

摘要

角蛋白是一种天然的生物聚合物，具有良好的生物相容性和生物可降解性。它被广泛应用于生物材料建筑中。角蛋白的二级结构在其应用中至关重要。这种结构与其再生有关。在本研究中，使用二阶导数傅立叶变换红外光谱中的酰胺I、II和III带分析了羊毛再生角蛋白的结构。结果表明，再生羊毛角蛋白通过二硫键的断裂保留了其分子骨架。酰胺I和II带表明，再生角蛋白中α-螺旋与非α-螺旋结构的含量比低于原毛。酰胺III带证实了原毛（35%/31%/22%/13%）和再生角蛋白（26%/35%/23%/15%）的α-螺旋/β-片/β-匝/无规卷曲的含量。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文本刊更多论文

Second-Order Derivation Fourier Transform Infrared Spectral Analysis of Regenerated Wool Keratin Structural Changes

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%).

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

AATCC Journal of Research MATERIALS SCIENCE, TEXTILES-

CiteScore

1.30

自引率

0.00%

发文量

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.