Cargando…

Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids

[Image: see text] An optimized reverse micelle surfactant system has been developed for solution nuclear magnetic resonance studies of encapsulated proteins and nucleic acids dissolved in low viscosity fluids. Comprising the nonionic 1-decanoyl-rac-glycerol and the zwitterionic lauryldimethylamine-N...

Descripción completa

Detalles Bibliográficos
Autores principales: Dodevski, Igor, Nucci, Nathaniel V., Valentine, Kathleen G., Sidhu, Gurnimrat K., O’Brien, Evan S., Pardi, Arthur, Wand, A. Joshua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3969725/
https://www.ncbi.nlm.nih.gov/pubmed/24495164
http://dx.doi.org/10.1021/ja410716w
_version_ 1782309307160723456
author Dodevski, Igor
Nucci, Nathaniel V.
Valentine, Kathleen G.
Sidhu, Gurnimrat K.
O’Brien, Evan S.
Pardi, Arthur
Wand, A. Joshua
author_facet Dodevski, Igor
Nucci, Nathaniel V.
Valentine, Kathleen G.
Sidhu, Gurnimrat K.
O’Brien, Evan S.
Pardi, Arthur
Wand, A. Joshua
author_sort Dodevski, Igor
collection PubMed
description [Image: see text] An optimized reverse micelle surfactant system has been developed for solution nuclear magnetic resonance studies of encapsulated proteins and nucleic acids dissolved in low viscosity fluids. Comprising the nonionic 1-decanoyl-rac-glycerol and the zwitterionic lauryldimethylamine-N-oxide (10MAG/LDAO), this mixture is shown to efficiently encapsulate a diverse set of proteins and nucleic acids. Chemical shift analyses of these systems show that high structural fidelity is achieved upon encapsulation. The 10MAG/LDAO surfactant system reduces the molecular reorientation time for encapsulated macromolecules larger than ∼20 kDa leading to improved overall NMR performance. The 10MAG/LDAO system can also be used for solution NMR studies of lipid-modified proteins. New and efficient strategies for optimization of encapsulation conditions are described. 10MAG/LDAO performs well in both the low viscosity pentane and ultralow viscosity liquid ethane and therefore will serve as a general surfactant system for initiating solution NMR studies of proteins and nucleic acids.
format Online
Article
Text
id pubmed-3969725
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher American Chemical Society
record_format MEDLINE/PubMed
spelling pubmed-39697252015-02-04 Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids Dodevski, Igor Nucci, Nathaniel V. Valentine, Kathleen G. Sidhu, Gurnimrat K. O’Brien, Evan S. Pardi, Arthur Wand, A. Joshua J Am Chem Soc [Image: see text] An optimized reverse micelle surfactant system has been developed for solution nuclear magnetic resonance studies of encapsulated proteins and nucleic acids dissolved in low viscosity fluids. Comprising the nonionic 1-decanoyl-rac-glycerol and the zwitterionic lauryldimethylamine-N-oxide (10MAG/LDAO), this mixture is shown to efficiently encapsulate a diverse set of proteins and nucleic acids. Chemical shift analyses of these systems show that high structural fidelity is achieved upon encapsulation. The 10MAG/LDAO surfactant system reduces the molecular reorientation time for encapsulated macromolecules larger than ∼20 kDa leading to improved overall NMR performance. The 10MAG/LDAO system can also be used for solution NMR studies of lipid-modified proteins. New and efficient strategies for optimization of encapsulation conditions are described. 10MAG/LDAO performs well in both the low viscosity pentane and ultralow viscosity liquid ethane and therefore will serve as a general surfactant system for initiating solution NMR studies of proteins and nucleic acids. American Chemical Society 2014-02-04 2014-03-05 /pmc/articles/PMC3969725/ /pubmed/24495164 http://dx.doi.org/10.1021/ja410716w Text en Copyright © 2014 American Chemical Society
spellingShingle Dodevski, Igor
Nucci, Nathaniel V.
Valentine, Kathleen G.
Sidhu, Gurnimrat K.
O’Brien, Evan S.
Pardi, Arthur
Wand, A. Joshua
Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids
title Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids
title_full Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids
title_fullStr Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids
title_full_unstemmed Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids
title_short Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids
title_sort optimized reverse micelle surfactant system for high-resolution nmr spectroscopy of encapsulated proteins and nucleic acids dissolved in low viscosity fluids
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3969725/
https://www.ncbi.nlm.nih.gov/pubmed/24495164
http://dx.doi.org/10.1021/ja410716w
work_keys_str_mv AT dodevskiigor optimizedreversemicellesurfactantsystemforhighresolutionnmrspectroscopyofencapsulatedproteinsandnucleicacidsdissolvedinlowviscosityfluids
AT nuccinathanielv optimizedreversemicellesurfactantsystemforhighresolutionnmrspectroscopyofencapsulatedproteinsandnucleicacidsdissolvedinlowviscosityfluids
AT valentinekathleeng optimizedreversemicellesurfactantsystemforhighresolutionnmrspectroscopyofencapsulatedproteinsandnucleicacidsdissolvedinlowviscosityfluids
AT sidhugurnimratk optimizedreversemicellesurfactantsystemforhighresolutionnmrspectroscopyofencapsulatedproteinsandnucleicacidsdissolvedinlowviscosityfluids
AT obrienevans optimizedreversemicellesurfactantsystemforhighresolutionnmrspectroscopyofencapsulatedproteinsandnucleicacidsdissolvedinlowviscosityfluids
AT pardiarthur optimizedreversemicellesurfactantsystemforhighresolutionnmrspectroscopyofencapsulatedproteinsandnucleicacidsdissolvedinlowviscosityfluids
AT wandajoshua optimizedreversemicellesurfactantsystemforhighresolutionnmrspectroscopyofencapsulatedproteinsandnucleicacidsdissolvedinlowviscosityfluids