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 Lettjournal_title
FEBS lettersauthors
Bortoleto RK,Ward RJdoi
10.1016/s0014-5793(99)01246-6keywords:
subject
Has Abstractpub_date
1999-10-15 00:00:00pages
438-42issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01246-6journal_volume
459pub_type
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