Sajda Ashraf , Hina Qaiser , Sumayya Tariq , Asaad Khalid , Hafiz A. Makeen , Hassan A. Alhazmi , Zaheer Ul-Haq
{"title":"揭示人血清白蛋白的多功能性——对其生物学意义和治疗潜力的全面综述","authors":"Sajda Ashraf , Hina Qaiser , Sumayya Tariq , Asaad Khalid , Hafiz A. Makeen , Hassan A. Alhazmi , Zaheer Ul-Haq","doi":"10.1016/j.crstbi.2023.100114","DOIUrl":null,"url":null,"abstract":"<div><p>Human serum albumin (HSA) is a multi-domain macromolecule with diverse ligand binding capability because of its ability to allow allosteric modulation despite being a monomeric protein. Physiologically, HSA act as the primary carrier for various exogenous and endogenous compounds and fatty acids, and alter the pharmacokinetic properties of several drugs. It has antioxidant properties and is utilized therapeutically to improve the drug delivery of pharmacological agents for the treatment of several disorders. The flexibility of albumin in holding various types of drugs coupled with a variety of modifications makes this protein a versatile drug carrier with incalculable potential in therapeutics. This review provides a brief outline of the different structural properties of HSA, and its various binding sites, moreover, an overview of the genetic, biomedical, and allosteric modulation of drugs and drug delivery aspects of HSA is also included, which may be helpful in guiding advanced clinical applications and further research on the therapeutic potential of this extraordinary protein.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"6 ","pages":"Article 100114"},"PeriodicalIF":2.7000,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X2300020X/pdfft?md5=b48d75ec4e200dc2416c06c820ca16bf&pid=1-s2.0-S2665928X2300020X-main.pdf","citationCount":"0","resultStr":"{\"title\":\"Unraveling the versatility of human serum albumin – A comprehensive review of its biological significance and therapeutic potential\",\"authors\":\"Sajda Ashraf , Hina Qaiser , Sumayya Tariq , Asaad Khalid , Hafiz A. Makeen , Hassan A. Alhazmi , Zaheer Ul-Haq\",\"doi\":\"10.1016/j.crstbi.2023.100114\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Human serum albumin (HSA) is a multi-domain macromolecule with diverse ligand binding capability because of its ability to allow allosteric modulation despite being a monomeric protein. Physiologically, HSA act as the primary carrier for various exogenous and endogenous compounds and fatty acids, and alter the pharmacokinetic properties of several drugs. It has antioxidant properties and is utilized therapeutically to improve the drug delivery of pharmacological agents for the treatment of several disorders. The flexibility of albumin in holding various types of drugs coupled with a variety of modifications makes this protein a versatile drug carrier with incalculable potential in therapeutics. This review provides a brief outline of the different structural properties of HSA, and its various binding sites, moreover, an overview of the genetic, biomedical, and allosteric modulation of drugs and drug delivery aspects of HSA is also included, which may be helpful in guiding advanced clinical applications and further research on the therapeutic potential of this extraordinary protein.</p></div>\",\"PeriodicalId\":10870,\"journal\":{\"name\":\"Current Research in Structural Biology\",\"volume\":\"6 \",\"pages\":\"Article 100114\"},\"PeriodicalIF\":2.7000,\"publicationDate\":\"2023-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.sciencedirect.com/science/article/pii/S2665928X2300020X/pdfft?md5=b48d75ec4e200dc2416c06c820ca16bf&pid=1-s2.0-S2665928X2300020X-main.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Research in Structural Biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2665928X2300020X\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Research in Structural Biology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2665928X2300020X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Unraveling the versatility of human serum albumin – A comprehensive review of its biological significance and therapeutic potential
Human serum albumin (HSA) is a multi-domain macromolecule with diverse ligand binding capability because of its ability to allow allosteric modulation despite being a monomeric protein. Physiologically, HSA act as the primary carrier for various exogenous and endogenous compounds and fatty acids, and alter the pharmacokinetic properties of several drugs. It has antioxidant properties and is utilized therapeutically to improve the drug delivery of pharmacological agents for the treatment of several disorders. The flexibility of albumin in holding various types of drugs coupled with a variety of modifications makes this protein a versatile drug carrier with incalculable potential in therapeutics. This review provides a brief outline of the different structural properties of HSA, and its various binding sites, moreover, an overview of the genetic, biomedical, and allosteric modulation of drugs and drug delivery aspects of HSA is also included, which may be helpful in guiding advanced clinical applications and further research on the therapeutic potential of this extraordinary protein.