Herein, we report the efficient exfoliation of MoS2 in aqueous medium by short cationic peptide nanotubes featuring the nucleating core 17LVFFA21 of β‐amyloid (Aβ 1–42), a sequence associated with Alzheimer's disease. The role of morphology, length, and nature of the amyloid surface on exfoliation/dispersions of MoS2 were investigated through specific mutations of the amyloid sequences. Notably, owing to the properties of both the constituents, self‐assembled soft nanostructures and MoS2, the hybrid dispersions responded reversibly to various stimuli, including temperature, pH, and light. Addition of a protease resulted in loss of the dispersions, which are otherwise stable for months at ambient conditions. The design flexibility of the peptide sequences, along with the stimuli‐responsiveness and biodegradability, can complement the applications of MoS2 in diverse fields.
Das effiziente Abblättern von MoS2‐Pulver gelingt in wässrigen Medien unter Verwendung von β‐Amyloid‐Nanoröhren. Die Peptidsequenz enthielt die zentrale Nukleationseinheit 17LVFFA21 von β‐Amyloid (Aβ 1–42). Durch die Eigenschaften von Amyloid und MoS2 reagierten auch die Hybriddispersionen auf verschiedene Reize, z. B. Temperatur, pH, Licht und Ionen.