Selectivity of Complex Coacervation in Multiprotein Mixtures.
Journal
JACS Au
ISSN: 2691-3704
Titre abrégé: JACS Au
Pays: United States
ID NLM: 101775714
Informations de publication
Date de publication:
28 Oct 2024
28 Oct 2024
Historique:
received:
03
05
2024
revised:
15
07
2024
accepted:
14
08
2024
medline:
1
11
2024
pubmed:
1
11
2024
entrez:
1
11
2024
Statut:
epublish
Résumé
Liquid-liquid phase separation of biomolecules is increasingly recognized as being relevant to various cellular functions, and complex coacervation of biomacromolecules, particularly proteins, is emerging as a key mechanism for this phenomenon. Complex coacervation is also being explored as a potential protein purification method due to its potential scalability, aqueous operation, and ability to produce a highly concentrated product. However, to date, most studies of complex coacervation have evaluated the phase behavior of a binary mixture of two oppositely charged macromolecules. Therefore, a comprehensive understanding of the phase behavior of complex biological mixtures is yet to be established. To address this, a panel of engineered proteins was designed to allow for quantitative analysis of the complex coacervation of individual proteins within a multicomponent mixture. The behavior of individual proteins was evaluated using a defined mixture of proteins that mimics the charge profile of the
Identifiants
pubmed: 39483238
doi: 10.1021/jacsau.4c00399
pmc: PMC11522905
doi:
Types de publication
Journal Article
Langues
eng
Pagination
3800-3812Informations de copyright
© 2024 The Authors. Published by American Chemical Society.
Déclaration de conflit d'intérêts
The authors declare the following competing financial interest(s): A.C.O. is a co-founder of Werewool, a company that is engaged in the development of performance textiles that incorporate engineered proteins. S.Y.A. declares no competing interests.