Understanding enzyme kinetics on coacervate as a substrate hub

Zhicheng Jin; Jesse V. Jokerst

doi:10.1117/12.3005376

13 March 2024 Understanding enzyme kinetics on coacervate as a substrate hub

Zhicheng Jin, Jesse V. Jokerst

Proceedings Volume 12859, Colloidal Nanoparticles for Biomedical Applications XIX; 1285903 (2024) https://doi.org/10.1117/12.3005376
Event: SPIE BiOS, 2024, San Francisco, California, United States

Abstract

There remains a gap in understanding the enzyme interactions with the coacervate as a substrate hub. Here, we study how the hydrophobicity nature of coacervate affects the interactions of the embedded substrate with a protease. We design oligopeptide-based coacervates that comprise an anionic Asp-peptide (D₁₀) and a cationic Arg-peptide (R₅R₅) with a proteolytic cleavage site. The coacervates dissolve when exposed to the main protease. We exploit the condensed structure, implement a self-quenching mechanism, and characterize enzyme kinetics with Cy5.5-labeled peptides. The determined specificity constant is 5,817 M^-1 s^-1 and is similar to that of the free substrate. We further show that the enzyme kinetics depend on the amount of dye incorporated into the coacervates. Our work presents a simple design for coacervates with tuned bioactivities and provides insights into the kinetics between the enzyme and coacervates as a substrate hub.

Conference Presentation

(2024) Published by SPIE. Downloading of the abstract is permitted for personal use only.

Citation Download Citation

Zhicheng Jin and Jesse V. Jokerst "Understanding enzyme kinetics on coacervate as a substrate hub", Proc. SPIE 12859, Colloidal Nanoparticles for Biomedical Applications XIX, 1285903 (13 March 2024); https://doi.org/10.1117/12.3005376

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