Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins

Yuri Hong; Saeed Najafi; Thomas Casey; Joan-Emma Shea; Song-I Han; Dong Soo Hwang

doi:10.1038/s41467-022-35001-1

Nature Communications (Nov 2022)

Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins

Yuri Hong,
Saeed Najafi,
Thomas Casey,
Joan-Emma Shea,
Song-I Han,
Dong Soo Hwang

Affiliations

Yuri Hong: School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology (POSTECH)
Saeed Najafi: Department of Chemistry & Biochemistry, University of California
Thomas Casey: Department of Chemistry & Biochemistry, University of California
Joan-Emma Shea: Department of Chemistry & Biochemistry, University of California
Song-I Han: Department of Chemistry & Biochemistry, University of California
Dong Soo Hwang: School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology (POSTECH)

DOI: https://doi.org/10.1038/s41467-022-35001-1
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 15

Abstract

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Arginine-rich proteins display reentrant LLPS behavior with changes in salt and temperature due to the hydrophobicity of arginine. Controlling the reentrant LLPS behavior opens avenues for the bioengineering and drug delivery fields.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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