Mohit Sharma, Artur P. Biela, Agnieszka Kowalczyk, Kinga Borzęcka-Solarz, Bernard M. A. G. Piette, Szymon Gaweł, Joshua Bishop, Philipp Kukura, Justin L. P. Benesch, Motonori Imamura, Simon Scheuring and Jonathan G. Heddle*,
{"title":"由单个氨基酸变化诱导的具有不寻常几何形状的人工蛋白质笼的形状-变形","authors":"Mohit Sharma, Artur P. Biela, Agnieszka Kowalczyk, Kinga Borzęcka-Solarz, Bernard M. A. G. Piette, Szymon Gaweł, Joshua Bishop, Philipp Kukura, Justin L. P. Benesch, Motonori Imamura, Simon Scheuring and Jonathan G. Heddle*, ","doi":"10.1021/acsnanoscienceau.2c00019","DOIUrl":null,"url":null,"abstract":"Artificial protein cages are constructed from multiple protein subunits. The interaction between the subunits, notably the angle formed between them, controls the geometry of the resulting cage. Here, using the artificial protein cage, “TRAP-cage”, we show that a simple alteration in the position of a single amino acid responsible for Au(I)-mediated subunit–subunit interactions in the constituent ring-shaped building blocks results in a more acute dihedral angle between them. In turn, this causes a dramatic shift in the structure from a 24-ring cage with an octahedral symmetry to a 20-ring cage with a C2 symmetry. This symmetry change is accompanied by a decrease in the number of Au(I)-mediated bonds between cysteines and a concomitant change in biophysical properties of the cage.","PeriodicalId":29799,"journal":{"name":"ACS Nanoscience Au","volume":null,"pages":null},"PeriodicalIF":4.8000,"publicationDate":"2022-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9585630/pdf/","citationCount":"4","resultStr":"{\"title\":\"Shape-Morphing of an Artificial Protein Cage with Unusual Geometry Induced by a Single Amino Acid Change\",\"authors\":\"Mohit Sharma, Artur P. Biela, Agnieszka Kowalczyk, Kinga Borzęcka-Solarz, Bernard M. A. G. Piette, Szymon Gaweł, Joshua Bishop, Philipp Kukura, Justin L. P. Benesch, Motonori Imamura, Simon Scheuring and Jonathan G. Heddle*, \",\"doi\":\"10.1021/acsnanoscienceau.2c00019\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Artificial protein cages are constructed from multiple protein subunits. The interaction between the subunits, notably the angle formed between them, controls the geometry of the resulting cage. Here, using the artificial protein cage, “TRAP-cage”, we show that a simple alteration in the position of a single amino acid responsible for Au(I)-mediated subunit–subunit interactions in the constituent ring-shaped building blocks results in a more acute dihedral angle between them. In turn, this causes a dramatic shift in the structure from a 24-ring cage with an octahedral symmetry to a 20-ring cage with a C2 symmetry. This symmetry change is accompanied by a decrease in the number of Au(I)-mediated bonds between cysteines and a concomitant change in biophysical properties of the cage.\",\"PeriodicalId\":29799,\"journal\":{\"name\":\"ACS Nanoscience Au\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.8000,\"publicationDate\":\"2022-05-09\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9585630/pdf/\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"ACS Nanoscience Au\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://pubs.acs.org/doi/10.1021/acsnanoscienceau.2c00019\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"NANOSCIENCE & NANOTECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Nanoscience Au","FirstCategoryId":"1085","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acsnanoscienceau.2c00019","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"NANOSCIENCE & NANOTECHNOLOGY","Score":null,"Total":0}
Shape-Morphing of an Artificial Protein Cage with Unusual Geometry Induced by a Single Amino Acid Change
Artificial protein cages are constructed from multiple protein subunits. The interaction between the subunits, notably the angle formed between them, controls the geometry of the resulting cage. Here, using the artificial protein cage, “TRAP-cage”, we show that a simple alteration in the position of a single amino acid responsible for Au(I)-mediated subunit–subunit interactions in the constituent ring-shaped building blocks results in a more acute dihedral angle between them. In turn, this causes a dramatic shift in the structure from a 24-ring cage with an octahedral symmetry to a 20-ring cage with a C2 symmetry. This symmetry change is accompanied by a decrease in the number of Au(I)-mediated bonds between cysteines and a concomitant change in biophysical properties of the cage.
期刊介绍:
ACS Nanoscience Au is an open access journal that publishes original fundamental and applied research on nanoscience and nanotechnology research at the interfaces of chemistry biology medicine materials science physics and engineering.The journal publishes short letters comprehensive articles reviews and perspectives on all aspects of nanoscience and nanotechnology:synthesis assembly characterization theory modeling and simulation of nanostructures nanomaterials and nanoscale devicesdesign fabrication and applications of organic inorganic polymer hybrid and biological nanostructuresexperimental and theoretical studies of nanoscale chemical physical and biological phenomenamethods and tools for nanoscience and nanotechnologyself- and directed-assemblyzero- one- and two-dimensional materialsnanostructures and nano-engineered devices with advanced performancenanobiotechnologynanomedicine and nanotoxicologyACS Nanoscience Au also publishes original experimental and theoretical research of an applied nature that integrates knowledge in the areas of materials engineering physics bioscience and chemistry into important applications of nanomaterials.