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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 1590 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 1580 | - |
dc.citation.title | BIOPHYSICAL JOURNAL | - |
dc.citation.volume | 76 | - |
dc.contributor.author | Renault, A | - |
dc.contributor.author | Lenne, PF | - |
dc.contributor.author | Zakri, C | - |
dc.contributor.author | Aradian, A | - |
dc.contributor.author | Venien-Bryan, C | - |
dc.contributor.author | Amblard, F | - |
dc.date.accessioned | 2023-12-22T12:11:57Z | - |
dc.date.available | 2023-12-22T12:11:57Z | - |
dc.date.created | 2020-01-31 | - |
dc.date.issued | 1999-03 | - |
dc.description.abstract | Living cells contain a very targe amount of membrane surface area, which potentially influences the direction, the kinetics, and the localization of biochemical reactions. This paper quantitatively evaluates the possibility that a lipid monolayer can adsorb actin from a nonpolymerizing solution, induce its polymerization, and form a 2D network of individual actin filaments in conditions that forbid bulk polymerization. G- and F-actin solutions were studied beneath saturated Langmuir monolayers containing phosphatidylcholine (PC, neutral) and stearylamine (SA, a positively charged surfactant) at PC:SA = 3:1 molar ratio. Ellipsometry, tensiometry, shear elastic measurements, electron microscopy, and dark-field tight microscopy were used to characterize the adsorption kinetics and the interfacial polymerization of actin. In all cases studied, actin follows a monoexponential reaction-limited adsorption with similar time constants (similar to 10(3) s). At a longer time scale the shear elasticity of the monomeric actin adsorbate increases only in the presence of lipids, to a 2D shear elastic modulus of mu approximate to 30 mN/m, indicating the formation of a structure coupled to the monolayer. Electron microscopy shows the formation of a 2D network of actin filaments at the PC:SA surface, and several arguments strongly suggest that this network is indeed causing the observed elasticity. Adsorption of F-actin to PC:SA leads more quickly to a silghtly more rigid interface with a modulus of mu approximate to 50 mN/m. | - |
dc.identifier.bibliographicCitation | BIOPHYSICAL JOURNAL, v.76, no.3, pp.1580 - 1590 | - |
dc.identifier.doi | 10.1016/S0006-3495(99)77317-0 | - |
dc.identifier.issn | 0006-3495 | - |
dc.identifier.scopusid | 2-s2.0-0033019678 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/31099 | - |
dc.identifier.url | https://www.sciencedirect.com/science/article/pii/S0006349599773170?via%3Dihub | - |
dc.identifier.wosid | 000078972300038 | - |
dc.language | 영어 | - |
dc.publisher | BIOPHYSICAL SOCIETY | - |
dc.title | Surface-induced polymerization of actin | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | POSITIVELY CHARGED LIPOSOMES | - |
dc.subject.keywordPlus | BINDING PROTEINS | - |
dc.subject.keywordPlus | DYNAMICS | - |
dc.subject.keywordPlus | NETWORKS | - |
dc.subject.keywordPlus | PARACRYSTALS | - |
dc.subject.keywordPlus | MONOLAYERS | - |
dc.subject.keywordPlus | RESOLUTION | - |
dc.subject.keywordPlus | FILAMENTS | - |
dc.subject.keywordPlus | MODULI | - |
dc.subject.keywordPlus | MODEL | - |
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