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

Microtubules are major cytoskeletons involved in various cellular functions, such as regulating cell shape and division and cargo transport motor proteins. In addition to widely studied singlet microtubules, complex microtubule superstructures, including doublets and bundles, provide unique mechanical and functional properties . However, a method to construct such superstructures remains unresolved.

Optical Control of Microtubule Accumulation and Dispersion by Tau-Derived Peptide-Fused Photoresponsive Protein.

Microtubules, a major component of the cytoskeleton consisting of tubulin dimers, are involved in various cellular functions, including forming axons and dendrites of neurons and retaining cell shapes by forming various accumulated superstructures such as bundles and doublets. Moreover, microtubule-accumulated structures like swarming microtubule assemblies are attractive components for dynamic materials, such as active matter and molecular robots. Thus, dynamic control of microtubule superstructures is an important topic.

Reversible Photocontrol of Microtubule Stability by Spiropyran-Conjugated Tau-Derived Peptides.

Spatiotemporal modulation of microtubules by light has become an important aspect of the biological and nanotechnological applications of microtubules. We previously developed a Tau-derived peptide as a binding unit to the inside of microtubules. Here, we conjugated the Tau-derived peptide to spiropyran, which is reversibly converted to merocyanine by light, as a reversible photocontrol system to stabilize microtubules.

Light-induced stabilization of microtubules by photo-crosslinking of a Tau-derived peptide.

For light-induced stabilization of microtubules (MTs) to manipulate cells, a photo-reactive diazirine group was conjugated to a Tau-derived peptide, a motif binding on the inside of MTs. Ultraviolet (UV) light irradiation induced significant stabilization of MTs the formation of a covalent bond of the peptide and showed toxicity.