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Updated: Jul 24, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
Published on: July 17, 2019
Voltage-calibrated, finely tunable protein assembly
Yin-Chen Lin1,2, Eloise Masquelier1,3, Yahya Al Sabeh1,4
1Institute for Collaborative Biotechnologies, University of California, Santa Barbara, CA 93106, USA.
Abstract:
Neuronally triggered phosphorylation drives the calibrated and cyclable assembly of the reflectin signal transducing proteins, resulting in their fine tuning of colours reflected from specialized skin cells in squid for camouflage and communication. In close parallel to this physiological behaviour, we demonstrate for the first time that electrochemical reduction of reflectin A1, used as a surrogate for charge neutralization by phosphorylation, triggers voltage-calibrated, proportional and cyclable control of the size of the protein's assembly. Electrochemically triggered condensation, folding and assembly were simultaneously analysed using in situ dynamic light scattering, circular dichroism and UV absorbance spectroscopies. The correlation of assembly size with applied potential is probably linked to reflectin's mechanism of dynamic arrest, which is controlled by the extent of neuronally triggered charge neutralization and the corresponding fine tuning of colour in the biological system. This work opens a new perspective on electrically controlling and simultaneously observing reflectin assembly and, more broadly, provides access to manipulate, observe and electrokinetically control the formation of intermediates and conformational dynamics of macromolecular systems.
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