Conformational Effects of Mutations and Spherical Confinement in Small Peptides through Hybrid Multi-Population Genetic Algorithms
Por:
Gonzalez-Olvera, Marcos A., Olivares-Quiroz, Luis
Publicada:
1 nov 2022
Ahead of Print:
1 ago 2022
Resumen:
In this work the role of spherical confinement combined with single and
block mutations in small peptides on the onset of specific
conformational states is analyzed. An intramolecular potential for the
polypeptide chain, composed by a bending term plus a Lennard-Jones type
long range potential is proposed. For the intermolecular interaction
with the sphere an integrated Lennard-Jones (LJ) type potential is used
between monomers and the sphere surface. To compute the set of minima
values for the total intra and intermolecular potential a combination of
a multi-population genetic algorithm and an hybridized Nelder-Mead
simplex algorithm are used, that yield to a larger degree of precision
in the prediction of the set of minima potential energy values. To
characterize the conformational states of the peptides the gyration
tensor, radius of gyration, the asphericity, and the linear anisotropy
are computed, and the influence of single-point and block mutations on
the most energetically stable conformations are assed. Results suggest
that the spherical confinement does have a significant influence of the
polymer conformations; and single-point mutations introduced along the
chain also have a prominent role on peptide's folded states. This opens
up the possibility to targeted-designed peptides with particular and
desired properties upon folding.
Filiaciones:
Gonzalez-Olvera, Marcos A.:
Univ Autonoma Ciudad Mexico UACM, Colegio Ciencia & Tecnol, Mexico City 09760, DF, Mexico
Olivares-Quiroz, Luis:
Univ Autonoma Ciudad Mexico UACM, Colegio Ciencia & Tecnol, Mexico City 09760, DF, Mexico
Univ Nacl Autonoma Mexico, Ctr Ciencias Complejidad C3, Mexico City 04510, DF, Mexico
|