Kunisato Kuroi, Yuta Kanazawa, Akane Shinaridome, Yuna Yasuda, Minkyo Jung, Chan-Gi Pack and Fumihiko Fujii
{"title":"不同形状的CdSe/CdS半导体纳米晶体上蛋白质电晕的形成。","authors":"Kunisato Kuroi, Yuta Kanazawa, Akane Shinaridome, Yuna Yasuda, Minkyo Jung, Chan-Gi Pack and Fumihiko Fujii","doi":"10.1039/D4NA00696H","DOIUrl":null,"url":null,"abstract":"<p >Nanoparticles (NPs) have been widely studied and applied in medical and pharmaceutical fields. When NPs enter the <em>in vivo</em> environment, they are covered with protein molecules to form the so-called “protein corona”. Because NPs and proteins are comparable in size, the shape of NPs has a significant impact on NP–protein interactions. Although NPs of various shapes have been synthesized, how the shape of NPs affects the protein corona is poorly understood, and little is known about the underlying molecular mechanism. In the present study, we synthesized spherical, football-shaped, and rod-shaped semiconductor nanocrystals (SNCs) as model NPs and compared their interaction with human serum albumin (HSA) using fluorescence correlation spectroscopy, fluorescence quenching, Fourier-transform infrared spectroscopy, and thermodynamic analysis. Based on the binding enthalpy and entropy and secondary structural changes of HSA, with the help of hydrodynamic diameter changes of SNCs, we concluded that HSA adopts a conformation or orientation that is appropriate for the local curvature of SNCs. This study demonstrates the effect of NP shape on their interaction with proteins and provides a mechanistic perspective.</p>","PeriodicalId":18806,"journal":{"name":"Nanoscale Advances","volume":" 2","pages":" 560-571"},"PeriodicalIF":4.6000,"publicationDate":"2024-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11621831/pdf/","citationCount":"0","resultStr":"{\"title\":\"Protein corona formation on different-shaped CdSe/CdS semiconductor nanocrystals†\",\"authors\":\"Kunisato Kuroi, Yuta Kanazawa, Akane Shinaridome, Yuna Yasuda, Minkyo Jung, Chan-Gi Pack and Fumihiko Fujii\",\"doi\":\"10.1039/D4NA00696H\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p >Nanoparticles (NPs) have been widely studied and applied in medical and pharmaceutical fields. When NPs enter the <em>in vivo</em> environment, they are covered with protein molecules to form the so-called “protein corona”. Because NPs and proteins are comparable in size, the shape of NPs has a significant impact on NP–protein interactions. Although NPs of various shapes have been synthesized, how the shape of NPs affects the protein corona is poorly understood, and little is known about the underlying molecular mechanism. In the present study, we synthesized spherical, football-shaped, and rod-shaped semiconductor nanocrystals (SNCs) as model NPs and compared their interaction with human serum albumin (HSA) using fluorescence correlation spectroscopy, fluorescence quenching, Fourier-transform infrared spectroscopy, and thermodynamic analysis. Based on the binding enthalpy and entropy and secondary structural changes of HSA, with the help of hydrodynamic diameter changes of SNCs, we concluded that HSA adopts a conformation or orientation that is appropriate for the local curvature of SNCs. This study demonstrates the effect of NP shape on their interaction with proteins and provides a mechanistic perspective.</p>\",\"PeriodicalId\":18806,\"journal\":{\"name\":\"Nanoscale Advances\",\"volume\":\" 2\",\"pages\":\" 560-571\"},\"PeriodicalIF\":4.6000,\"publicationDate\":\"2024-11-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11621831/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nanoscale Advances\",\"FirstCategoryId\":\"88\",\"ListUrlMain\":\"https://pubs.rsc.org/en/content/articlelanding/2025/na/d4na00696h\",\"RegionNum\":3,\"RegionCategory\":\"材料科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nanoscale Advances","FirstCategoryId":"88","ListUrlMain":"https://pubs.rsc.org/en/content/articlelanding/2025/na/d4na00696h","RegionNum":3,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Protein corona formation on different-shaped CdSe/CdS semiconductor nanocrystals†
Nanoparticles (NPs) have been widely studied and applied in medical and pharmaceutical fields. When NPs enter the in vivo environment, they are covered with protein molecules to form the so-called “protein corona”. Because NPs and proteins are comparable in size, the shape of NPs has a significant impact on NP–protein interactions. Although NPs of various shapes have been synthesized, how the shape of NPs affects the protein corona is poorly understood, and little is known about the underlying molecular mechanism. In the present study, we synthesized spherical, football-shaped, and rod-shaped semiconductor nanocrystals (SNCs) as model NPs and compared their interaction with human serum albumin (HSA) using fluorescence correlation spectroscopy, fluorescence quenching, Fourier-transform infrared spectroscopy, and thermodynamic analysis. Based on the binding enthalpy and entropy and secondary structural changes of HSA, with the help of hydrodynamic diameter changes of SNCs, we concluded that HSA adopts a conformation or orientation that is appropriate for the local curvature of SNCs. This study demonstrates the effect of NP shape on their interaction with proteins and provides a mechanistic perspective.