Electroosmotic enhancement of the binding of a neutral molecule to a transmembrane pore.
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| Title: | Electroosmotic enhancement of the binding of a neutral molecule to a transmembrane pore. |
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| Authors: | Li-Qun Gu1, Cheley, Stephen1, Bayley, Hagan1,2,3 bayley@tamu.edu |
| Source: | Proceedings of the National Academy of Sciences of the United States of America. 12/23/2003, Vol. 100 Issue 26, p15498-15503. 6p. |
| Subjects: | Proteins, Electroosmotic dewatering, Ions, Electro-osmosis, Water, Biomolecules |
| Abstract: | The flux of solvent water coupled to the transit of ions through protein pores is considerable. The effect of this electroosmotic solvent flow on the binding of a neutral molecule [β-cyclodextrin (βCD)] to sites within the staphylococcal α-hemolysin pore was investigated. Mutant α-hemolysin pores were used to which βCD can bind from either entrance and through which the direction of water flow can be controlled by choosing the charge selectivity of the pore and the polarity of the applied potential. The Kd values for βCD for individual mutant pores varied by >100-fold with the applied potential over a range of -120 to + 120 mV. In all cases, the signs of the changes in binding free energy and the influence of potential on the association and dissociation rate constants for βCD were consistent with an electroosmotic effect. [ABSTRACT FROM AUTHOR] |
| Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 12109929 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Electroosmotic enhancement of the binding of a neutral molecule to a transmembrane pore. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Li-Qun+Gu%22">Li-Qun Gu</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Cheley%2C+Stephen%22">Cheley, Stephen</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Bayley%2C+Hagan%22">Bayley, Hagan</searchLink><relatesTo>1,2,3</relatesTo><i> bayley@tamu.edu</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America%22">Proceedings of the National Academy of Sciences of the United States of America</searchLink>. 12/23/2003, Vol. 100 Issue 26, p15498-15503. 6p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Electroosmotic+dewatering%22">Electroosmotic dewatering</searchLink><br /><searchLink fieldCode="DE" term="%22Ions%22">Ions</searchLink><br /><searchLink fieldCode="DE" term="%22Electro-osmosis%22">Electro-osmosis</searchLink><br /><searchLink fieldCode="DE" term="%22Water%22">Water</searchLink><br /><searchLink fieldCode="DE" term="%22Biomolecules%22">Biomolecules</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: The flux of solvent water coupled to the transit of ions through protein pores is considerable. The effect of this electroosmotic solvent flow on the binding of a neutral molecule [β-cyclodextrin (βCD)] to sites within the staphylococcal α-hemolysin pore was investigated. Mutant α-hemolysin pores were used to which βCD can bind from either entrance and through which the direction of water flow can be controlled by choosing the charge selectivity of the pore and the polarity of the applied potential. The Kd values for βCD for individual mutant pores varied by >100-fold with the applied potential over a range of -120 to + 120 mV. In all cases, the signs of the changes in binding free energy and the influence of potential on the association and dissociation rate constants for βCD were consistent with an electroosmotic effect. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1073/pnas.2531778100 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 6 StartPage: 15498 Subjects: – SubjectFull: Proteins Type: general – SubjectFull: Electroosmotic dewatering Type: general – SubjectFull: Ions Type: general – SubjectFull: Electro-osmosis Type: general – SubjectFull: Water Type: general – SubjectFull: Biomolecules Type: general Titles: – TitleFull: Electroosmotic enhancement of the binding of a neutral molecule to a transmembrane pore. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Li-Qun Gu – PersonEntity: Name: NameFull: Cheley, Stephen – PersonEntity: Name: NameFull: Bayley, Hagan IsPartOfRelationships: – BibEntity: Dates: – D: 23 M: 12 Text: 12/23/2003 Type: published Y: 2003 Identifiers: – Type: issn-print Value: 00278424 Numbering: – Type: volume Value: 100 – Type: issue Value: 26 Titles: – TitleFull: Proceedings of the National Academy of Sciences of the United States of America Type: main |
| ResultId | 1 |
