Spontaneous Formation of Cushioned Model Membranes Promoted by an Intrinsically Disordered Protein
In this article, it is shown that by exposing commonly used lipids for biomembrane mimicking studies, to a solution containing the histidine-rich intrinsically disordered protein histatin 5, a protein cushion spontaneously forms underneath the bilayer. The underlying mechanism is attributed to have...
| Publié dans: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 36(2020), 15 vom: 21. Apr., Seite 3997-4004 |
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| Auteur principal: | |
| Autres auteurs: | , , , , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2020
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| Accès à la collection: | Langmuir : the ACS journal of surfaces and colloids |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't Intrinsically Disordered Proteins Lipid Bilayers |
| Résumé: | In this article, it is shown that by exposing commonly used lipids for biomembrane mimicking studies, to a solution containing the histidine-rich intrinsically disordered protein histatin 5, a protein cushion spontaneously forms underneath the bilayer. The underlying mechanism is attributed to have an electrostatic origin, and it is hypothesized that the observed behavior is due to proton charge fluctuations promoting attractive electrostatic interactions between the positively charged proteins and the anionic surfaces, with concomitant counterion release. Hence, we anticipate that this novel "green" approach of forming cushioned bilayers can be an important tool to mimic the cell membrane without the disturbance of the solid substrate, thereby achieving a further understanding of protein-cell interactions |
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| Description: | Date Completed 21.06.2021 Date Revised 09.12.2022 published: Print-Electronic ErratumIn: Langmuir. 2022 Dec 20;38(50):15888. doi: 10.1021/acs.langmuir.2c03141. - PMID 36493364 Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.0c00120 |