The interaction between heparin and Lys49 phospholipase A(2) reveals the natural binding of heparin on the enzyme

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorBugs, M. R.
dc.creatorBortoleto-Bugs, R. K.
dc.creatorCornelio, M. L.
dc.date2014-05-20T14:02:24Z
dc.date2016-10-25T17:09:05Z
dc.date2014-05-20T14:02:24Z
dc.date2016-10-25T17:09:05Z
dc.date2005-10-30
dc.date.accessioned2017-04-05T21:27:29Z
dc.date.available2017-04-05T21:27:29Z
dc.identifierInternational Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 37, n. 1-2, p. 21-27, 2005.
dc.identifier0141-8130
dc.identifierhttp://hdl.handle.net/11449/21998
dc.identifierhttp://acervodigital.unesp.br/handle/11449/21998
dc.identifier10.1016/j.ijbiomac.2005.08.003
dc.identifierWOS:000233283800003
dc.identifierhttp://dx.doi.org/10.1016/j.ijbiomac.2005.08.003
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/867473
dc.descriptionWe have studied at a molecular level the interaction of heparins on bothropstoxin-1 (BthTx-1), a phospholipase A(2) toxin. The protein was monitored using gel filtration chromatography, dynamic light scattering (DLS), circular dichroism (CD), attenuated total reflectance Fourier transform infrared (ATR-FTIR) and intrinsic tryptophan fluorescence emission (ITFE) spectroscopy. The elution profile of the protein presents a displacement of the protein peak to larger complexes when interacting with higher concentration of heparin. The DLS results shows two R-h at a molar ratio of 1, one to the distribution of the protein and the second for the action of heparin on BthTx-I structures, and a large distribution with the increase of protein. The interaction is accompanied by significant changes in the CD spectra, showing two common features: a decrease in signal at 208 nm (3 and 6 kDa heparins) and an isodichroic point near 226 nm (3 kDa heparin). FTIR spectra indicate that only a few amino acid residues are involved in this interaction. Alterations in the ITFE by binding heparins suggest that the initial binding occurs on the ventral face of BthTx-1. Together, these results add an experimental and structural basis on the action mechanism of the heparins over the phospholipases A(2) and provide a molecular model to elucidate the interaction of the enzyme-heparin complex at a molecular level. (c) 2005 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationInternational Journal of Biological Macromolecules
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectheparin
dc.subjectphospholipase A(2)
dc.subjectFTIR spectroscopy
dc.subjectmolecular model
dc.titleThe interaction between heparin and Lys49 phospholipase A(2) reveals the natural binding of heparin on the enzyme
dc.typeOtro


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