Capturing coacervate formation and protein partition by molecular dynamics simulation

Yang Liu; Xinyan Wang; Zhili Wan; To Ngai; Ying-Lung Steve Tse

doi:10.1039/d2sc01164f

Capturing coacervate formation and protein partition by molecular dynamics simulation

Chem Sci. 2022 Dec 24;14(5):1168-1175. doi: 10.1039/d2sc01164f. eCollection 2023 Feb 1.

Authors

Yang Liu^{1

2}, Xinyan Wang², Zhili Wan³, To Ngai², Ying-Lung Steve Tse²

Affiliations

¹ College of Polymer Science and Engineering, State Key Laboratory of Polymer Materials Engineering, Sichuan University Chengdu 610065 China.
² Department of Chemistry, The Chinese University of Hong Kong Sha Tin Hong Kong China tongai@cuhk.edu.hk stevetse@cuhk.edu.hk.
³ School of Food Science and Engineering, South China University of Technology Guangzhou China.

Abstract

Biomolecules localize and function in microenvironments where their local concentration, spatial organization, and biochemical reactivity are regulated. To compartmentalize and control the local properties of the native microenvironment, cellular mimics and artificial bioreactors have been developed to study the properties of membraneless organelles or mimic the bio-environment for life origin. Here, we carried out molecular dynamics simulation with the Martini 3.0 model to reproduce the experimental salt concentration and pH dependency of different complex coacervates. We showed that coacervates inside vesicles are able to change their shape. In addition, we used these coacervate systems to explore the partitioning of the ubiquitous cytoskeletal protein actin and found that actin spontaneously partitions to all the coacervate peripheries. Therefore, we believe that our study can provide a better understanding of the versatile coacervate platform, where biomolecules partition and gather to fulfill their biological duties.