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Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses
This article is related to http://dx.doi.org/10.1016/j.bbamem.2017.01.005 (Ø. Strømland, Ø.S. Handegård, M.L. Govasli, H. Wen, Ø. Halskau, 2017) [1]. In protein and polypeptide-membrane interaction studies, negatively charged lipids are often used as they are a known driver for membrane interaction....
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5384297/ https://www.ncbi.nlm.nih.gov/pubmed/28413816 http://dx.doi.org/10.1016/j.dib.2017.03.014 |
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author | Strømland, Øyvind Handegård, Ørjan S. Govasli, Morten L. Wen, Hanzhen Furse, Samuel Halskau, Øyvind |
author_facet | Strømland, Øyvind Handegård, Ørjan S. Govasli, Morten L. Wen, Hanzhen Furse, Samuel Halskau, Øyvind |
author_sort | Strømland, Øyvind |
collection | PubMed |
description | This article is related to http://dx.doi.org/10.1016/j.bbamem.2017.01.005 (Ø. Strømland, Ø.S. Handegård, M.L. Govasli, H. Wen, Ø. Halskau, 2017) [1]. In protein and polypeptide-membrane interaction studies, negatively charged lipids are often used as they are a known driver for membrane interaction. When using fluorescence spectroscopy and CD as indicators of polypeptide binding and conformational change, respectively, the effect of zwitterionic lipids only should be documented. The present data documents several aspects of how two engineered polypeptides (A-Cage-C and A-Lnk-C) derived from the membrane associating protein alpha-Lactalbumin affects and are affected by the presence of zwitterionic bilayers in the form of vesicles. We here document the behavior or the Cage and Lnk segments with respect to membrane interaction and their residual fold, using intrinsic tryptophan fluorescence assays. This data description also documents the coverage of solid-supported bilayers prepared by spin-coating mica using binary lipid mixes, a necessary step to ensure that AFM is performed on areas that are covered by lipid bilayers when performing experiments. Uncovered patches are detectable by both force curve measurements and height measurements. We tested naked mica׳s ability to cause aggregation as seen by AFM, and found this to be low compared to preparations containing negatively charged lipids. Work with lipids also carries the risk of chemical degradation taking place during vesicles preparation or other handling of the lipids. We therefor use (31)P NMR to quantify the head-group content of commonly used commercial extracts before and after a standard protocol for vesicle production is applied. |
format | Online Article Text |
id | pubmed-5384297 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-53842972017-04-14 Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses Strømland, Øyvind Handegård, Ørjan S. Govasli, Morten L. Wen, Hanzhen Furse, Samuel Halskau, Øyvind Data Brief Data Article This article is related to http://dx.doi.org/10.1016/j.bbamem.2017.01.005 (Ø. Strømland, Ø.S. Handegård, M.L. Govasli, H. Wen, Ø. Halskau, 2017) [1]. In protein and polypeptide-membrane interaction studies, negatively charged lipids are often used as they are a known driver for membrane interaction. When using fluorescence spectroscopy and CD as indicators of polypeptide binding and conformational change, respectively, the effect of zwitterionic lipids only should be documented. The present data documents several aspects of how two engineered polypeptides (A-Cage-C and A-Lnk-C) derived from the membrane associating protein alpha-Lactalbumin affects and are affected by the presence of zwitterionic bilayers in the form of vesicles. We here document the behavior or the Cage and Lnk segments with respect to membrane interaction and their residual fold, using intrinsic tryptophan fluorescence assays. This data description also documents the coverage of solid-supported bilayers prepared by spin-coating mica using binary lipid mixes, a necessary step to ensure that AFM is performed on areas that are covered by lipid bilayers when performing experiments. Uncovered patches are detectable by both force curve measurements and height measurements. We tested naked mica׳s ability to cause aggregation as seen by AFM, and found this to be low compared to preparations containing negatively charged lipids. Work with lipids also carries the risk of chemical degradation taking place during vesicles preparation or other handling of the lipids. We therefor use (31)P NMR to quantify the head-group content of commonly used commercial extracts before and after a standard protocol for vesicle production is applied. Elsevier 2017-03-12 /pmc/articles/PMC5384297/ /pubmed/28413816 http://dx.doi.org/10.1016/j.dib.2017.03.014 Text en © 2017 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Data Article Strømland, Øyvind Handegård, Ørjan S. Govasli, Morten L. Wen, Hanzhen Furse, Samuel Halskau, Øyvind Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses |
title | Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses |
title_full | Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses |
title_fullStr | Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses |
title_full_unstemmed | Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses |
title_short | Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses |
title_sort | spectroscopic and afm characterization of polypeptide-surface interactions: controls and lipid quantitative analyses |
topic | Data Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5384297/ https://www.ncbi.nlm.nih.gov/pubmed/28413816 http://dx.doi.org/10.1016/j.dib.2017.03.014 |
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