# Peptide-mediated display of Tau-derived peptide for construction of microtubule superstructures

## TL;DR

Researchers developed a method to build microtubule superstructures in the lab using peptides, offering new insights into their formation and potential applications in nanotechnology.

## Contribution

A novel peptide-based strategy to construct microtubule superstructures in vitro using KA7 peptides and Tau-derived peptides.

## Key findings

- KA7–TP binds to microtubules and induces the formation of doublets and bundles.
- Outer layers of doublet microtubules generated by KA7–TP can dissociate, aiding in studying their dynamics.
- The method provides a simple and effective approach for constructing and analyzing microtubule superstructures.

## Abstract

Microtubules are major cytoskeletons involved in various cellular functions, such as regulating cell shape and division and cargo transport via motor proteins. In addition to widely studied singlet microtubules, complex microtubule superstructures, including doublets and bundles, provide unique mechanical and functional properties in vivo. However, a method to construct such superstructures in vitro remains unresolved. This study presents a peptide-based approach for constructing microtubule superstructures by displaying Tau-derived peptides (TP) on the outer surface of microtubules using KA7 peptides as binding units. The KA7-connected TP (KA7–TP) bound to the C-terminal tail on the outer surface of microtubules and induced doublets and bundles by recruiting tubulin. Notably, the outer layers of the doublet microtubules generated by KA7–TP dissociated, highlighting the utility of this approach for studying the formation/dissociation mechanisms of microtubule superstructures. The simple peptide-based approach facilitates our understanding of microtubule superstructures and offers new opportunities for applying microtubule superstructures to nanotechnology.

Microtubule superstructures including doublet microtubules were constructed by displaying Tau-derived peptide on the surface of microtubules using cationic KA7 peptide.