The assembling and contraction mechanisms of striated muscles
- 1Duke University, United States
A novel approach to the description of the assembly mechanism of functional biological structures is presented. The approach is based on the identification of fundamental self-assembling processes to which an additional structurization “engineered” by Nature to optimize functions is superimposed. Application of the approach to the structure and contraction of the striated muscle evidences a key role of the residual liquid crystallinity of a constrained structure and the alteration of the compatibility between the thin and thick filaments driven by ionic interactions. ATP hydrolysis boosts the relaxation process. A strong protein scaffold, engineered during the evolutionary process and based on the selective anchoring of coordinated filaments, directs a demixing tendency of the two filaments toward a sliding motion along the fiber axis. The Huxley-Hanson sliding filament hypothesis aimed to explain the contraction-relaxation function of the striated muscle, but does not offer any clue on the overall assembling mechanism of the myofibril.
Keywords: striated muscle, self-assembly, Actin, Myosin, Titin, Sarcomers, Liquid crystallinity, polyelectrolyte-salt interaction, Polymer compatibility
Received: 14 Sep 2018;
Accepted: 02 Nov 2018.
Edited by:CLaudia Caltagirone, Università degli studi di Cagliari, Italy
Reviewed by:Xiao-Yu Hu, Nanjing University of Aeronautics and Astronautics, China
Xiaojun Shi, Case Western Reserve University, United States
Copyright: © 2018 Ciferri and Crumbliss. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Prof. Alberto Ciferri, Duke University, Durham, United States, firstname.lastname@example.org