Jinyue Fan, Mingcong Xu, Wei Li, Bang An, Shouxin Liu
{"title":"Preparation of tryptophan-derived chiral carbon quantum dots by hydrothermal carbonization and their chiral recognition properties","authors":"Jinyue Fan, Mingcong Xu, Wei Li, Bang An, Shouxin Liu","doi":"10.1360/ssc-2023-0232","DOIUrl":"https://doi.org/10.1360/ssc-2023-0232","url":null,"abstract":"","PeriodicalId":515091,"journal":{"name":"SCIENTIA SINICA Chimica","volume":"210 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140275876","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
: Collagen is the most abundant protein in the human body. Over 90% of its total content is heterotrimers. Mutation of glycine in any polypeptide chain of natural heterotrimeric collagen will lead to genetic diseases. Due to the large molecular weight and complex structure of collagen, it is challenging to investigate collagen at the molecular level. Collagen peptides have been widely contributed to mimic collagen. Due to their small molecular weight and easily controlled structure, heterotrimeric collagen peptides can precisely mimic the chain composition, structure, and function of heterotrimeric collagen, such as type I and type IV collagen. This review describes in detail the design, characterization, and applications of heterotrimeric collagen peptides. Firstly, two strategies for constructing heterotrimeric collagen peptides have been summarized, involving covalent bonding and non-covalent interactions. Secondly, the methods for characterizing chain composition, triple helical structure, and thermal stability of heterotrimeric collagen peptides have been outlined. Furthermore, the application areas of heterotrimeric collagen peptides in simulating the chain registers and fibrous structure of collagen, as well as investigating the mechanisms of osteogenesis imperfecta, have been introduced. Finally, an outlook on the development of functionalized heterotrimeric collagen peptides and their potential applications in the field of biomedical research has been proposed.
:胶原蛋白是人体内含量最丰富的蛋白质。其总含量的 90% 以上是异源三聚体。天然异三聚胶原蛋白多肽链中任何一个甘氨酸的突变都会导致遗传疾病。由于胶原蛋白分子量大、结构复杂，从分子水平研究胶原蛋白具有挑战性。胶原蛋白肽被广泛用于模拟胶原蛋白。由于分子量小、结构易于控制，异三聚胶原蛋白肽可以精确地模拟异三聚胶原蛋白（如 I 型和 IV 型胶原蛋白）的链组成、结构和功能。本综述详细介绍了异三聚胶原蛋白肽的设计、表征和应用。首先，总结了构建异三聚胶原蛋白肽的两种策略，包括共价键和非共价相互作用。其次，概述了表征异三聚胶原蛋白肽的链组成、三重螺旋结构和热稳定性的方法。此外，还介绍了异三聚胶原蛋白肽在模拟胶原蛋白的链注册和纤维结构以及研究成骨不全症机制方面的应用领域。最后，展望了功能化异三聚胶原蛋白肽的发展及其在生物医学研究领域的潜在应用。
{"title":"Heterotrimeric collagen peptides: design, characterization, and applications","authors":"Siqi Quan, Lanyue Zhang, Ziyong Zhang, Xiuxia Sun, Jianxi Xiao","doi":"10.1360/ssc-2023-0218","DOIUrl":"https://doi.org/10.1360/ssc-2023-0218","url":null,"abstract":": Collagen is the most abundant protein in the human body. Over 90% of its total content is heterotrimers. Mutation of glycine in any polypeptide chain of natural heterotrimeric collagen will lead to genetic diseases. Due to the large molecular weight and complex structure of collagen, it is challenging to investigate collagen at the molecular level. Collagen peptides have been widely contributed to mimic collagen. Due to their small molecular weight and easily controlled structure, heterotrimeric collagen peptides can precisely mimic the chain composition, structure, and function of heterotrimeric collagen, such as type I and type IV collagen. This review describes in detail the design, characterization, and applications of heterotrimeric collagen peptides. Firstly, two strategies for constructing heterotrimeric collagen peptides have been summarized, involving covalent bonding and non-covalent interactions. Secondly, the methods for characterizing chain composition, triple helical structure, and thermal stability of heterotrimeric collagen peptides have been outlined. Furthermore, the application areas of heterotrimeric collagen peptides in simulating the chain registers and fibrous structure of collagen, as well as investigating the mechanisms of osteogenesis imperfecta, have been introduced. Finally, an outlook on the development of functionalized heterotrimeric collagen peptides and their potential applications in the field of biomedical research has been proposed.","PeriodicalId":515091,"journal":{"name":"SCIENTIA SINICA Chimica","volume":"25 10","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140277679","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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