title: Differential effect of solution conditions on the conformation of the actinoporins Sticholysin II and Equinatoxin II.
abstract: Actinoporins are a family of pore-forming proteins with hemolytic activity. The structural basis for such activity appears to depend on their correct folding. Such folding encompasses a phosphocholine binding site, a tryptophan-rich region and the activity-related N-terminus segment. Additionally, different solution conditions are known to be able to influence the pore formation by actinoporins, as for Sticholysin II (StnII) and Equinatoxin II (EqtxII). In this context, the current work intends to characterize the influence of distinct solution conditions in the conformational behavior of these proteins through molecular dynamics (MD) simulations. The obtained data offer structural insights into actinoporins dynamics in solution, characterizing its conformational behavior at the atomic level, in accordance with previous experimental data on StnII and EqtxII hemolytic activities.
authors.affiliation: Centro de Biotecnologia, UFRGS, Porto Alegre, RS, Brasil.
authors.forename: Edson V F
authors.initials: EV
authors.lastname: Fauth
authors.affiliation: Departamento de Bioquímica e Tecnologia Química, UNESP, Instituto de Química, Universidade Estadual Paulista, Araraquara, SP, Brasil.
authors.forename: Eduardo M
authors.initials: EM
authors.lastname: Cilli
authors.affiliation: Centro de Biotecnologia, UFRGS, Porto Alegre, RS, Brasil.
authors.forename: Rodrigo
authors.initials: R
authors.lastname: Ligabue-Braun
authors.affiliation: Centro de Biotecnologia, UFRGS, Porto Alegre, RS, Brasil.
authors.forename: Hugo
authors.initials: H
authors.lastname: Verli
mesh_terms: D003064:Cnidarian Venoms / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D003064:Cnidarian Venoms; C404794:sticholysin II; C012307:equinatoxin