Conformational changes of Loxosceles venom sphingomyelinases monitored by circular dichroism

Conformational changes of Loxosceles venom sphingomyelinases monitored by circular dichroism

Author Andrade, S. A. de Google Scholar
Pedrosa, MFF Google Scholar
Andrade, RMG de Google Scholar
Oliva, MLV Google Scholar
van den Berge, C. W. Google Scholar
Tambourgi, D. V. Google Scholar
Institution Inst Butantan
Universidade Federal de São Paulo (UNIFESP)
Cardiff Univ
Abstract Envenomation by arachnids of the genus Loxosceles can induce a variety of biological effects, including dermonecrosis and hemolysis. We have previously identified in L. intermedia venom two highly homologous proteins with sphingomyelinase activity, termed P1 and P2, responsible for all these pathological events, and also an inactive isoform P3. the toxins P1 and P2 displayed 85% identity with each other at the amino acid level and showed a 57% identity with SMase I, an active toxin from L. laeta venom. Circular dichroism was used to determine and compare the solution structure of the active and inactive isoforms. Effects of pH and temperature change on the CD spectra of the toxins were investigated and correlated with the biological activities. This study sheds new light on the structure-function relationship of homologous proteins with distinct biological properties and represents the first report on the structure-function relationship of Loxosceles sphingomyelinases D. (C) 2004 Elsevier Inc. All rights reserved.
Keywords Loxosceles
circular dichroism
sphingomyelinase D
Language English
Date 2005-02-04
Published in Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 327, n. 1, p. 117-123, 2005.
ISSN 0006-291X (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 117-123
Access rights Closed access
Type Article
Web of Science ID WOS:000226345400019

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