A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus.

Abstract:

:The effects of mildly acidic conditions on the free energy of unfolding (DeltaG(u)(buff)) of the pore-forming alpha-hemolysin (alphaHL) from Staphylococcus aureus were assessed between pH 5.0 and 7.5 by measuring intrinsic tryptophan fluorescence, circular dichroism and elution time in size exclusion chromatography during urea denaturation. Decreasing the pH from 7.0 to 5.0 reduced the calculated DeltaG(u)(buff) from 8.9 to 4.2 kcal mol(-1), which correlates with an increased rate of pore formation previously observed over the same pH range. It is proposed that the lowered surface pH of biological membranes reduces the stability of alphaHL thereby modulating the rate of pore formation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Bortoleto RK,Ward RJ

doi

10.1016/s0014-5793(99)01246-6

keywords:

subject

Has Abstract

pub_date

1999-10-15 00:00:00

pages

438-42

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)01246-6

journal_volume

459

pub_type

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