z-logo
open-access-imgOpen Access
An adapted particle swarm optimization algorithm as a model for exploring premyofibril formation
Author(s) -
William F. Sherman,
Anna Grosberg
Publication year - 2020
Publication title -
aip advances
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.421
H-Index - 58
ISSN - 2158-3226
DOI - 10.1063/1.5145010
Subject(s) - myofibril , biological system , particle swarm optimization , process (computing) , swarm behaviour , computer science , biophysics , chemistry , microbiology and biotechnology , algorithm , biology , artificial intelligence , biochemistry , operating system
While the fundamental steps outlining myofibril formation share a similar scheme for different cell and species types, various granular details involved in the development of a functional contractile muscle are not well understood. Many studies of myofibrillogenesis focus on the protein interactions that are involved in myofibril maturation with the assumption that there is a fully formed premyofibril at the start of the process. However, there is little known regarding how the premyofibril is initially constructed. Fortunately, the protein α -actinin, which has been consistently identified throughout the maturation process, is found in premyofibrils as punctate aggregates known as z-bodies. We propose a theoretical model based on the particle swarm optimization algorithm that can explore how these α -actinin clusters form into the patterns observed experimentally. Our algorithm can produce different pattern configurations by manipulating specific parameters that can be related to α -actinin mobility and binding affinity. These patterns, which vary experimentally according to species and muscle cell type, speak to the versatility of α -actinin and demonstrate how its behavior may be altered through interactions with various regulatory, signaling, and metabolic proteins. The results of our simulations invite speculation that premyofibrils can be influenced toward developing different patterns by altering the behavior of individual α -actinin molecules, which may be linked to key differences present in different cell types.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom