Differential Effect of Solution Conditions on the Conformation of the Actinoporins Sticholysin II and Equinatoxin II

作者：Fauth Edson V F; Cilli Eduardo M; Ligabue Braun Rodrigo; Verli Hugo^*

来源：ANAIS DA ACADEMIA BRASILEIRA DE CIENCIAS, 2014, 86(4): 1949-1962.

DOI：10.1590/0001-3765201420140270

• Actinoporins
• GROMACS
• Molecular dynamics
• Pore-forming proteins

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.

• 出版日期2014-12
• 单位Univ Estadual Paulista