Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters.
In this study, the charge selectivity of staphylococcal alpha-hemolysin (alphaHL), a bacterial pore-forming toxin, is manipulated by using cyclodextrins as noncovalent molecular adapters. Anion-selective versions of alphaHL, including the wild-type pore and various mutants, become more anion selecti...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2000
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| _version_ | 1797077035417337856 |
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| author | Gu, L Dalla Serra, M Vincent, J Vigh, G Cheley, S Braha, O Bayley, H |
| author_facet | Gu, L Dalla Serra, M Vincent, J Vigh, G Cheley, S Braha, O Bayley, H |
| author_sort | Gu, L |
| collection | OXFORD |
| description | In this study, the charge selectivity of staphylococcal alpha-hemolysin (alphaHL), a bacterial pore-forming toxin, is manipulated by using cyclodextrins as noncovalent molecular adapters. Anion-selective versions of alphaHL, including the wild-type pore and various mutants, become more anion selective when beta-cyclodextrin (betaCD) is lodged within the channel lumen. By contrast, the negatively charged adapter, hepta-6-sulfato-beta-cyclodextrin (s(7)betaCD), produces cation selectivity. The cyclodextrin adapters have similar effects when placed in cation-selective mutant alphaHL pores. Most probably, hydrated Cl(-) ions partition into the central cavity of betaCD more readily than K(+) ions, whereas s(7)betaCD introduces a charged ring near the midpoint of the channel lumen and confers cation selectivity through electrostatic interactions. The molecular adapters generate permeability ratios (P(K+)/P(Cl-)) over a 200-fold range and should be useful in the de novo design of membrane channels both for basic studies of ion permeation and for applications in biotechnology. |
| first_indexed | 2024-03-07T00:12:01Z |
| format | Journal article |
| id | oxford-uuid:798f09e3-24e5-4c4a-a038-add9c3e10d7d |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:12:01Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:798f09e3-24e5-4c4a-a038-add9c3e10d7d2022-03-26T20:38:11ZReversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:798f09e3-24e5-4c4a-a038-add9c3e10d7dEnglishSymplectic Elements at Oxford2000Gu, LDalla Serra, MVincent, JVigh, GCheley, SBraha, OBayley, HIn this study, the charge selectivity of staphylococcal alpha-hemolysin (alphaHL), a bacterial pore-forming toxin, is manipulated by using cyclodextrins as noncovalent molecular adapters. Anion-selective versions of alphaHL, including the wild-type pore and various mutants, become more anion selective when beta-cyclodextrin (betaCD) is lodged within the channel lumen. By contrast, the negatively charged adapter, hepta-6-sulfato-beta-cyclodextrin (s(7)betaCD), produces cation selectivity. The cyclodextrin adapters have similar effects when placed in cation-selective mutant alphaHL pores. Most probably, hydrated Cl(-) ions partition into the central cavity of betaCD more readily than K(+) ions, whereas s(7)betaCD introduces a charged ring near the midpoint of the channel lumen and confers cation selectivity through electrostatic interactions. The molecular adapters generate permeability ratios (P(K+)/P(Cl-)) over a 200-fold range and should be useful in the de novo design of membrane channels both for basic studies of ion permeation and for applications in biotechnology. |
| spellingShingle | Gu, L Dalla Serra, M Vincent, J Vigh, G Cheley, S Braha, O Bayley, H Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters. |
| title | Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters. |
| title_full | Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters. |
| title_fullStr | Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters. |
| title_full_unstemmed | Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters. |
| title_short | Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters. |
| title_sort | reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters |
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