Improving Internal Peptide Dynamics in the Coarse-Grained MARTINI Model : Toward Large-Scale Simulations of Amyloid- and Elastin-like Peptides

Improving Internal Peptide Dynamics in the Coarse-Grained MARTINI Model : Toward Large-Scale Simulations of Amyloid- and Elastin-like Peptides. Seo, M., Rauscher, S., & Tieleman, D., P. Journal of Chemical Theory and Computation, 8(5):1774-1785, 2012.

Paper abstract bibtex 6 downloads

We present an extension of the coarse-grained MARTINI model for proteins and apply this extension to amyloidand elastin-like peptides. Atomistic simulations of tetrapeptides, octapeptides, and longer peptides in solution are used as a reference to parametrize a set of pseudodihedral potentials that describe the internal ﬂexibility of MARTINI peptides. We assess the performance of the resulting model in reproducing various structural properties computed from atomistic trajectories of peptides in water. The addition of new dihedral angle potentials improves agreement with the contact maps computed from atomistic simulations signiﬁcantly. We also address the question of which parameters derived from atomistic trajectories are transferable between diﬀerent lengths of peptides. The modiﬁed coarse-grained model shows reasonable transferability of parameters for the amyloid- and elastin-like peptides. In addition, the improved coarse-grained model is also applied to investigate the self-assembly of β-sheet forming peptides on the microsecond time scale. The octapeptides SNNFGAIL and (GV)4 are used to examine peptide aggregation in diﬀerent environments, in water, and at the water−octane interface. At the interface, peptide adsorption occurs rapidly, and peptides spontaneously aggregate in favor of stretched conformers resembling β-strands.

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 title = {Improving Internal Peptide Dynamics in the Coarse-Grained MARTINI Model : Toward Large-Scale Simulations of Amyloid- and Elastin-like Peptides},
 type = {article},
 year = {2012},
 pages = {1774-1785},
 volume = {8},
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 created = {2012-04-09T20:15:58.000Z},
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 abstract = {We present an extension of the coarse-grained MARTINI model for proteins and apply this extension to amyloidand elastin-like peptides. Atomistic simulations of tetrapeptides, octapeptides, and longer peptides in solution are used as a reference to parametrize a set of pseudodihedral potentials that describe the internal ﬂexibility of MARTINI peptides. We assess the performance of the resulting model in reproducing various structural properties computed from atomistic trajectories of peptides in water. The addition of new dihedral angle potentials improves agreement with the contact maps computed from atomistic simulations signiﬁcantly. We also address the question of which parameters derived from atomistic trajectories are transferable between diﬀerent lengths of peptides. The modiﬁed coarse-grained model shows reasonable transferability of parameters for the amyloid- and elastin-like peptides. In addition, the improved coarse-grained model is also applied to investigate the self-assembly of β-sheet forming peptides on the microsecond time scale. The octapeptides SNNFGAIL and (GV)4 are used to examine peptide aggregation in diﬀerent environments, in water, and at the water−octane interface. At the interface, peptide adsorption occurs rapidly, and peptides spontaneously aggregate in favor of stretched conformers resembling β-strands.},
 bibtype = {article},
 author = {Seo, Mikyung and Rauscher, Sarah and Tieleman, D Peter},
 journal = {Journal of Chemical Theory and Computation},
 number = {5}
}

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