Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/162100
Title: In vivo liquid-liquid phase separation protects amyloidogenic and aggregation-prone peptides during overexpression in Escherichia coli
Authors: Gabryelczyk, Bartosz
Alag, Reema
Philips, Margaret
Low, Kimberly
Venkatraman, Anandalakshmi
Kannaian, Bhuvaneswari
Shi, Xiangyan
Linder, Markus
Pervushin, Konstantin
Miserez, Ali
Keywords: Engineering::Materials
Science::Biological sciences
Issue Date: 2022
Source: Gabryelczyk, B., Alag, R., Philips, M., Low, K., Venkatraman, A., Kannaian, B., Shi, X., Linder, M., Pervushin, K. & Miserez, A. (2022). In vivo liquid-liquid phase separation protects amyloidogenic and aggregation-prone peptides during overexpression in Escherichia coli. Protein Science, 31(5), e4292-. https://dx.doi.org/10.1002/pro.4292
Project: MOE 2019-T3-1-012 
Journal: Protein Science
Abstract: Studying pathogenic effects of amyloids requires homogeneous amyloidogenic peptide samples. Recombinant production of these peptides is challenging due to their susceptibility to aggregation and chemical modifications. Thus, chemical synthesis is primarily used to produce amyloidogenic peptides suitable for high-resolution structural studies. Here, we exploited the shielded environment of protein condensates formed via liquid-liquid phase separation (LLPS) as a protective mechanism against premature aggregation. We designed a fusion protein tag undergoing LLPS in Escherichia coli and linked it to highly amyloidogenic peptides, including β amyloids. We find that the fusion proteins form membraneless organelles during overexpression and remain fluidic-like. We also developed a facile purification method of functional Aβ peptides free of chromatography steps. The strategy exploiting LLPS can be applied to other amyloidogenic, hydrophobic, and repetitive peptides that are otherwise difficult to produce.
URI: https://hdl.handle.net/10356/162100
ISSN: 0961-8368
DOI: 10.1002/pro.4292
Rights: © 2022 The Protein Society. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:MSE Journal Articles
SBS Journal Articles

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