Protein transfer into nanoscale compartments is critical for many cellular/life processes yet there has been no report on how compartment properties impact the protein orientation during a transfer. Such a knowledge gap limits a deeper understanding of protein transfer mechanism, which could be bridged through artificial porous materials. Here we employed a mesoporous silica, a covalent-organic framework, and a metal-organic framework with charged, hydrophobic, and neutral surfaces, respectively, to elucidate the impact of channel properties on the transfer of a model protein, lysozyme. Using site-directed spin labeling and time-resolved Electron Paramagnetic Resonance spectroscopy, we revealed that the transfer can be a multi-step process depending on channel properties and depicted the relative orientation changes of lysozyme upon transfer into each channel. This is the first structural insight into protein orientation upon transfer into different compartments, meaningful for the rational design of synthetic materials to host enzymes or mimic the cellular compartments.

In situ monitoring the protein transfer into artificial nanoscale channels

ACS Spring 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.