Endoproteolysis of Oligopeptide-Based Coacervates for Enzymatic Modeling.
Peptide coacervates
disassembly
energy transfer
enzyme kinetics
main protease
Journal
ACS nano
ISSN: 1936-086X
Titre abrégé: ACS Nano
Pays: United States
ID NLM: 101313589
Informations de publication
Date de publication:
12 09 2023
12 09 2023
Historique:
pmc-release:
12
09
2024
medline:
14
9
2023
pubmed:
14
8
2023
entrez:
14
8
2023
Statut:
ppublish
Résumé
Better insights into the fate of membraneless organelles could strengthen the understanding of the transition from prebiotic components to multicellular organisms. Compartmentalized enzyme reactions in a synthetic coacervate have been investigated, yet there remains a gap in understanding the enzyme interactions with coacervate as a substrate hub. Here, we study how the molecularly crowded nature of the coacervate affects the interactions of the embedded substrate with a protease. We design oligopeptide-based coacervates that comprise an anionic Asp-peptide (D
Identifiants
pubmed: 37579082
doi: 10.1021/acsnano.3c04259
pmc: PMC10614163
mid: NIHMS1937680
doi:
Substances chimiques
Proteins
0
Peptides
0
Oligopeptides
0
Peptide Hydrolases
EC 3.4.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
16980-16992Subventions
Organisme : NIDCR NIH HHS
ID : R01 DE031114
Pays : United States
Organisme : NIA NIH HHS
ID : R21 AG065776
Pays : United States
Organisme : NIAID NIH HHS
ID : R21 AI157957
Pays : United States
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