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Folding propensity of anoplin: A molecular dynamics study of the native peptide and four mutated isoforms
Author(s) -
Aschi Massimiliano,
Luzi Carla,
Fiorillo Annarita,
Bozzi Argante
Publication year - 2015
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22714
Subject(s) - chemistry , molecular dynamics , folding (dsp implementation) , peptide , gene isoform , amide , helix (gastropod) , cationic polymerization , protein folding , solvent , biophysics , crystallography , stereochemistry , computational chemistry , biochemistry , organic chemistry , ecology , electrical engineering , gene , engineering , biology , snail
Anoplin, a cationic decapeptide amide GLLKRIKTLL‐NH 2 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. © 2015 Wiley Periodicals, Inc. Biopolymers 103: 692–701, 2015.