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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

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pH-triggered disassembly in a caged protein complex.

Mercè Dalmau¹, Sierin Lim, Szu-Wen Wang

¹Department of Chemical Engineering and Materials Science, University of California, Irvine, California 92697-2575, USA.

Biomacromolecules

|October 31, 2009

Summary

Researchers engineered protein cages for targeted drug delivery. By incorporating histidines, they achieved pH-controlled disassembly, enabling precise molecular cargo release within cells for nanotechnology applications.

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Area of Science:

Biotechnology
Nanotechnology
Structural Biology

Background:

Self-assembling protein cages offer potential in nanotechnology, particularly for therapeutic delivery.
pH-controlled disassembly is crucial for targeted intracellular drug release from virus-like particles.

Purpose of the Study:

To engineer pH-dependent disassembly in protein cages using histidines.
To investigate the role of specific subunit interfaces in protein cage stability and disassembly.
To modulate the pH transition point for controlled cargo release.

Main Methods:

Redesign of two key subunit interfaces in the E2 subunit of pyruvate dehydrogenase.
Site-directed mutagenesis to introduce histidine residues at specific interfaces.
Analysis of protein cage stability and pH-triggered disassembly under varying ionic strengths.

Main Results:

Introducing histidine at the methionine-425 interface did not compromise protein cage stability.
Mutagenesis of the N-terminus and ionic strength adjustments enabled engineering of pH-dependent disassembly.
Histidine protonation-induced electrostatic repulsions were identified as the mechanism for pH-triggered disassembly.

Conclusions:

Altering electrostatic repulsions at subunit interfaces is a viable strategy for designing pH-triggered protein assembly.
This approach can be broadly applied to create responsive protein macromolecular structures for nanotechnology and drug delivery.