TAILIEUCHUNG - Báo cáo khoa học: Intrinsic local disorder and a network of charge–charge interactions are key to actinoporin membrane disruption and cytotoxicity

Actinoporins are a family of sea anemone proteins that bind to membranes and produce functional pores which result in cell lysis. Actinoporin vari-ants with decreased lytic activity usually show a reduced affinity for mem-branes. | 1FEBS Journal Intrinsic local disorder and a network of charge-charge interactions are key to actinoporin membrane disruption and cytotoxicity Miguel A. Pardo-Cea1 Ines Castrillo1 Jorge Alegre-Cebollada2 f Alvaro Martinez-del-Pozo2 Jose G. Gavilanes2 and Marta Bruix1 1 Departamento de Quimica Fisica Biologica Institute de Quimica Fisica Rocasolano Madrid Spain 2 Departamento de Bioquimica y Biologia Molecular I Facultad de Quimica Universidad Complutense Madrid Spain Keywords actinoporin dynamics electrostatic interactions NMR structure sticholysin Correspondence M. Bruix Departamento de Quimica Fisica Biologica Instituto de Quimica Fisica Rocasolano CSIC Serrano 119 28006 Madrid Spain Fax 34 91 561 9400 Tel 34 91 745 9511 E-mail mbruix@ These two authors contributed equally to this work ỶPresent address Department of Biological Sciences Columbia University New York USA Received 1 February 2011 revised 10 March 2011 accepted 1 April 2011 doi Actinoporins are a family of sea anemone proteins that bind to membranes and produce functional pores which result in cell lysis. Actinoporin variants with decreased lytic activity usually show a reduced affinity for membranes. However for some of these mutant versions there is no direct correlation between the loss of binding affinity and the decrease in their overall lytic activity suggesting that other steps in pore formation may be hampered or facilitated by the mutations. To test this hypothesis on the mechanism of pore formation by this interesting family of proteins structural and dynamic NMR studies have been carried out on two disabled variants of the actinoporin Sticholysin II R29Q and Y111N. It is shown that their lytic activity is not only related to their membrane affinity but also to their conformational mechanism for membrane insertion. Alterations in their activities can be explained by structural electrostatic and dynamic differences in a cluster of aromatic moieties

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