Charge engineering controls cooperative assembly and loading in protein host–guest complexes

2025/01/01 by Zhiheng Wang, Dai-Bei Yang, Joshua A. Bulos +5 · 1 voice
Biochemistry, Genetics and Molecular Biology · Physics and Astronomy · #Biochemical and Structural Characterization #Force Microscopy Techniques and Applications #Protein Structure and Dynamics

paper · pdf · doi:10.1039/d5tb01202c

openalex publication_date 2025/01/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01

Abstract

ferritin. Guided by molecular dynamics (MD) simulations and computational protein design, experiments confirmed that GFP charge magnitude and distribution dictate capsule assembly and loading efficiency. These data provide the first example of cooperative assembly with a ferritin capsule. Finally, we established a strategy for generating stoichiometric 1 : 1 protein host-guest complexes, confirmed by time-resolved fluorescence anisotropy. This provides a blueprint for designing ferritin host-guest complexes with enhanced homogeneity and functionality.

Citations

• CHARMM‐GUI: A web‐based graphical user interface for CHARMM
• Improvements to the APBS biomolecular solvation software suite
• Scalable molecular dynamics on CPU and GPU architectures with NAMD

Discussions

• Issue 30 for @JMaterChem C front cover features article "Charge engineering controls cooperative assembly and loading in protein host–guest complexes" by Ivan J. Dmochowski et al. Read their article [bsky, 0 points, 0 comments]