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His(1)-tagged DM or DDM detergent micelles are reversibly conjugated by nickel ions
Specific conjugation of decyl β-D-maltoside (DM) or dodecyl β-D-maltoside (DDM) detergent micelles is accomplished between pH 7.0–8.5 in the presence of an amphiphilic analog of the amino acid histidine, bound to a 10-carbon hydrocarbon chain (His(1)-C10) and Ni(2+) ions. Following addition of 10–15...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10564902/ https://www.ncbi.nlm.nih.gov/pubmed/37816812 http://dx.doi.org/10.1038/s41598-023-44236-x |
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author | Lal, Mitra Wachtel, Ellen Pati, Soumyaranjan Namboothiri, Irishi. N. N. Patchornik, Guy |
author_facet | Lal, Mitra Wachtel, Ellen Pati, Soumyaranjan Namboothiri, Irishi. N. N. Patchornik, Guy |
author_sort | Lal, Mitra |
collection | PubMed |
description | Specific conjugation of decyl β-D-maltoside (DM) or dodecyl β-D-maltoside (DDM) detergent micelles is accomplished between pH 7.0–8.5 in the presence of an amphiphilic analog of the amino acid histidine, bound to a 10-carbon hydrocarbon chain (His(1)-C10) and Ni(2+) ions. Following addition of 10–15 wt% PEG-6000 as precipitant, phase separation in the form of oil-rich globules (30–600 µm) is observed by light microscopy. Other divalent cations: Zn(2+), Fe(2+), Cu(2+) lead to dark precipitates rather than colorless globules; while Mg(2+), Ca(2+) do not promote any phase separation at all. Even in the absence of precipitant, dynamic light scattering (DLS) measurements demonstrate that DM micelles (hydrodynamic size ~ 6 nm) or DDM micelles (8 nm) self-associate into larger particles (9 nm and 411 nm for DM; 10 nm and 982 nm for DDM) in the presence of His(1)-C10 and nickel ions. Micellar conjugation is partially reversible in the presence of water soluble 50 mM EDTA, histidine or imidazole chelators. Cryo-transmission electron microscopy (cryo-TEM) imaging revealed the formation of non-uniformly dense detergent aggregates for both DM and DDM micelles in the presence of precipitant. The possible utility of such His(1)-tagged DM or DDM micelles for promoting crystallization of integral membrane proteins is discussed. |
format | Online Article Text |
id | pubmed-10564902 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-105649022023-10-12 His(1)-tagged DM or DDM detergent micelles are reversibly conjugated by nickel ions Lal, Mitra Wachtel, Ellen Pati, Soumyaranjan Namboothiri, Irishi. N. N. Patchornik, Guy Sci Rep Article Specific conjugation of decyl β-D-maltoside (DM) or dodecyl β-D-maltoside (DDM) detergent micelles is accomplished between pH 7.0–8.5 in the presence of an amphiphilic analog of the amino acid histidine, bound to a 10-carbon hydrocarbon chain (His(1)-C10) and Ni(2+) ions. Following addition of 10–15 wt% PEG-6000 as precipitant, phase separation in the form of oil-rich globules (30–600 µm) is observed by light microscopy. Other divalent cations: Zn(2+), Fe(2+), Cu(2+) lead to dark precipitates rather than colorless globules; while Mg(2+), Ca(2+) do not promote any phase separation at all. Even in the absence of precipitant, dynamic light scattering (DLS) measurements demonstrate that DM micelles (hydrodynamic size ~ 6 nm) or DDM micelles (8 nm) self-associate into larger particles (9 nm and 411 nm for DM; 10 nm and 982 nm for DDM) in the presence of His(1)-C10 and nickel ions. Micellar conjugation is partially reversible in the presence of water soluble 50 mM EDTA, histidine or imidazole chelators. Cryo-transmission electron microscopy (cryo-TEM) imaging revealed the formation of non-uniformly dense detergent aggregates for both DM and DDM micelles in the presence of precipitant. The possible utility of such His(1)-tagged DM or DDM micelles for promoting crystallization of integral membrane proteins is discussed. Nature Publishing Group UK 2023-10-10 /pmc/articles/PMC10564902/ /pubmed/37816812 http://dx.doi.org/10.1038/s41598-023-44236-x Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Lal, Mitra Wachtel, Ellen Pati, Soumyaranjan Namboothiri, Irishi. N. N. Patchornik, Guy His(1)-tagged DM or DDM detergent micelles are reversibly conjugated by nickel ions |
title | His(1)-tagged DM or DDM detergent micelles are reversibly conjugated by nickel ions |
title_full | His(1)-tagged DM or DDM detergent micelles are reversibly conjugated by nickel ions |
title_fullStr | His(1)-tagged DM or DDM detergent micelles are reversibly conjugated by nickel ions |
title_full_unstemmed | His(1)-tagged DM or DDM detergent micelles are reversibly conjugated by nickel ions |
title_short | His(1)-tagged DM or DDM detergent micelles are reversibly conjugated by nickel ions |
title_sort | his(1)-tagged dm or ddm detergent micelles are reversibly conjugated by nickel ions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10564902/ https://www.ncbi.nlm.nih.gov/pubmed/37816812 http://dx.doi.org/10.1038/s41598-023-44236-x |
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