Tandem malonate-based glucosides (TMGs) for membrane protein structural studies
Abstract High-resolution membrane protein structures are essential for understanding the molecular basis of diverse biological events and important in drug development. Detergents are usually used to extract these bio-macromolecules from the membranes and maintain them in a soluble and stable state...
Guardado en:
Autores principales: | , , , , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2017
|
Materias: | |
Acceso en línea: | https://doaj.org/article/087002c5c6c2415c9ebf4a39ab6e0c4d |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:087002c5c6c2415c9ebf4a39ab6e0c4d |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:087002c5c6c2415c9ebf4a39ab6e0c4d2021-12-02T16:07:57ZTandem malonate-based glucosides (TMGs) for membrane protein structural studies10.1038/s41598-017-03809-32045-2322https://doaj.org/article/087002c5c6c2415c9ebf4a39ab6e0c4d2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03809-3https://doaj.org/toc/2045-2322Abstract High-resolution membrane protein structures are essential for understanding the molecular basis of diverse biological events and important in drug development. Detergents are usually used to extract these bio-macromolecules from the membranes and maintain them in a soluble and stable state in aqueous solutions for downstream characterization. However, many eukaryotic membrane proteins solubilized in conventional detergents tend to undergo structural degradation, necessitating the development of new amphiphilic agents with enhanced properties. In this study, we designed and synthesized a novel class of glucoside amphiphiles, designated tandem malonate-based glucosides (TMGs). A few TMG agents proved effective at both stabilizing a range of membrane proteins and extracting proteins from the membrane environment. These favourable characteristics, along with synthetic convenience, indicate that these agents have potential in membrane protein research.Hazrat HussainJonas S. MortensenYang DuClaudia SantillanOrquidea RibeiroJuyeon GoParameswaran HariharanClaus J. LolandLan GuanBrian K. KobilkaBernadette ByrnePil Seok ChaeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Medicine R Science Q |
spellingShingle |
Medicine R Science Q Hazrat Hussain Jonas S. Mortensen Yang Du Claudia Santillan Orquidea Ribeiro Juyeon Go Parameswaran Hariharan Claus J. Loland Lan Guan Brian K. Kobilka Bernadette Byrne Pil Seok Chae Tandem malonate-based glucosides (TMGs) for membrane protein structural studies |
description |
Abstract High-resolution membrane protein structures are essential for understanding the molecular basis of diverse biological events and important in drug development. Detergents are usually used to extract these bio-macromolecules from the membranes and maintain them in a soluble and stable state in aqueous solutions for downstream characterization. However, many eukaryotic membrane proteins solubilized in conventional detergents tend to undergo structural degradation, necessitating the development of new amphiphilic agents with enhanced properties. In this study, we designed and synthesized a novel class of glucoside amphiphiles, designated tandem malonate-based glucosides (TMGs). A few TMG agents proved effective at both stabilizing a range of membrane proteins and extracting proteins from the membrane environment. These favourable characteristics, along with synthetic convenience, indicate that these agents have potential in membrane protein research. |
format |
article |
author |
Hazrat Hussain Jonas S. Mortensen Yang Du Claudia Santillan Orquidea Ribeiro Juyeon Go Parameswaran Hariharan Claus J. Loland Lan Guan Brian K. Kobilka Bernadette Byrne Pil Seok Chae |
author_facet |
Hazrat Hussain Jonas S. Mortensen Yang Du Claudia Santillan Orquidea Ribeiro Juyeon Go Parameswaran Hariharan Claus J. Loland Lan Guan Brian K. Kobilka Bernadette Byrne Pil Seok Chae |
author_sort |
Hazrat Hussain |
title |
Tandem malonate-based glucosides (TMGs) for membrane protein structural studies |
title_short |
Tandem malonate-based glucosides (TMGs) for membrane protein structural studies |
title_full |
Tandem malonate-based glucosides (TMGs) for membrane protein structural studies |
title_fullStr |
Tandem malonate-based glucosides (TMGs) for membrane protein structural studies |
title_full_unstemmed |
Tandem malonate-based glucosides (TMGs) for membrane protein structural studies |
title_sort |
tandem malonate-based glucosides (tmgs) for membrane protein structural studies |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/087002c5c6c2415c9ebf4a39ab6e0c4d |
work_keys_str_mv |
AT hazrathussain tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT jonassmortensen tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT yangdu tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT claudiasantillan tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT orquidearibeiro tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT juyeongo tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT parameswaranhariharan tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT clausjloland tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT languan tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT briankkobilka tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT bernadettebyrne tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies AT pilseokchae tandemmalonatebasedglucosidestmgsformembraneproteinstructuralstudies |
_version_ |
1718384636804988928 |