Folding propensity of anoplin: A molecular dynamics study of the native peptide and four mutated isoforms.
Anoplin, a cationic decapeptide amide GLLKRIKTLL-NH2 derived from venom sac of the solitary wasp Anoplius samariensis has been investigated through Molecular Dynamics. The wild-type (WT) and four isoforms were simulated both in water and in the membrane-mimicking solvent trifluoroethanol (TFE). In water all the investigated species, found to be in rapid equilibrium between different conformational states, can be considered as unfolded. On the other hand, in TFE all the systems enhance their rigidity and, in general, show α-helix as the main folded conformation. Interestingly, a semi-quantitative thermodynamic analysis has suggested that the folding driving force is not always the same being in some cases (e.g., the WT Anoplin) of entropic nature and in other cases of energetic nature.
Dipartimento Di Scienze Fisiche e Chimiche, University of L'Aquila, L'Aquila, Italy.
Massimiliano
M
Aschi
Department of Biotechnological and Applied Clinical Sciences, University of L'aquila, L'aquila, Italy.
Carla
C
Luzi
Department of Biochemical Sciences "Rossi-Fanelli", University of Rome "Sapienza", Rome, Italy.|Institute of Molecular Biology and Pathology, CNR, Rome, Italy.|Institute Pasteur Cenci-Bolognetti Foundation, Rome, Italy.
Annarita
A
Fiorillo
Department of Biotechnological and Applied Clinical Sciences, University of L'aquila, L'aquila, Italy.|Consorzio INBB, Rome, Italy.
Argante
A
Bozzi
D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000235:genetics*; D056004:Molecular Dynamics Simulation; D017510:Protein Folding; D020033:Protein Isoforms / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary; D014862:Wasp Venoms / Q000737:chemistry* / Q000235:genetics*
D023181:Antimicrobial Cationic Peptides; D020033:Protein Isoforms; D014862:Wasp Venoms; C443041:anoplin
anoplin; folding; molecular dynamics