Biomolecular condensates formed by designer minimalistic peptides

Avigail Baruch Leshem, Sian Sloan-Dennison, Tlalit Massarano, Shavit Ben-David, Duncan Graham, Karen Faulds, Hugo E. Gottlieb, Jordan H. Chill () and Ayala Lampel ()
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Avigail Baruch Leshem: Tel Aviv University
Sian Sloan-Dennison: University of Strathclyde
Tlalit Massarano: Tel Aviv University
Shavit Ben-David: Tel Aviv University
Duncan Graham: University of Strathclyde
Karen Faulds: University of Strathclyde
Hugo E. Gottlieb: Bar Ilan University
Jordan H. Chill: Bar Ilan University
Ayala Lampel: Tel Aviv University

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract Inspired by the role of intracellular liquid-liquid phase separation (LLPS) in formation of membraneless organelles, there is great interest in developing dynamic compartments formed by LLPS of intrinsically disordered proteins (IDPs) or short peptides. However, the molecular mechanisms underlying the formation of biomolecular condensates have not been fully elucidated, rendering on-demand design of synthetic condensates with tailored physico-chemical functionalities a significant challenge. To address this need, here we design a library of LLPS-promoting peptide building blocks composed of various assembly domains. We show that the LLPS propensity, dynamics, and encapsulation efficiency of compartments can be tuned by changes to the peptide composition. Specifically, with the aid of Raman and NMR spectroscopy, we show that interactions between arginine and aromatic amino acids underlie droplet formation, and that both intra- and intermolecular interactions dictate droplet dynamics. The resulting sequence-structure-function correlation could support the future development of compartments for a variety of applications.

Date: 2023
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DOI: 10.1038/s41467-023-36060-8

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