Abstract：
:Bothropstoxin-I (BthTx-I) is a homodimeric Lys49-PLA2 from the venom of the snake Bothrops jararacussu, which lacks hydrolytic activity against phospholipid substrates, yet permeabilizes membranes by a Ca2+-independent mechanism. The interaction of the BthTx-I with model membranes has been studied by intrinsic tryptophan fluorescence emission (ITFE) spectroscopy. Nine separate mutants have been created each with a unique tryptophan residue located at a different position in the interfacial recognition site (IRS) of the protein. The rapid and efficient Ca2+-independent membrane damage against unilamellar liposomes composed of DPPC/DMPA in a 9:1 molar ratio was unaffected by these substitutions. Binding studies revealed low protein affinity for these liposomes and no changes were observed in the ITFE properties. In contrast, the binding of all mutants to DPPC/DMPA liposomes in a 1:1 molar ratio was stronger, and was correlated with altered ITFE properties. The blue-shifted emission spectra and increased emission intensity of mutants at positions 31, 67 and 115-117 in the interface recognition surface of the protein suggest these regions are partially inserted into the membrane. These results are consistent with a model for the Ca2+-independent membrane damaging mechanism that involves a transient interaction of the protein with the outer phospholipid leaflet of the target membrane.
journal_name
Biochimiejournal_title
Biochimieauthors
Ferreira TL,Ruller R,Chioato L,Ward RJdoi
10.1016/j.biochi.2007.10.012subject
Has Abstractpub_date
2008-09-01 00:00:00pages
1397-406issue
9eissn
0300-9084issn
1638-6183pii
S0300-9084(07)00306-9journal_volume
90pub_type
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