Along with recent progress of nanotechnology, concern has risen about biological impacts of nanoparticles deriving from their interaction with cell membranes. Nanoparticles tend to adsorb proteins in vivo. Therefore, the physical properties of the conjugates to cell membranes must be investigated to elucidate and assess their properties. We examined whether one-dimensional protein-based nanoparticles induce liposome leakage in physiological saline. Carbon nanotube conjugates with adsorbed lysozyme interacted with the liposome through electrostatic interaction, leading to liposome leakage. Surprisingly, amyloid fibrils of lysozyme resembled the conjugate in terms of their effects on liposome leakage. Results described herein provide new insight into the interaction between nanoparticles and cell membranes in terms of their shape, mechanical properties, and noncovalent interactions.

In this article, we discuss the effects of amino acids on amyloid aggregation of lysozyme. l-cysteine (Cys) dramatically inhibited fibrillation of lysozyme, whereas other amino acids (including l-arginine) did not. In the presence of Cys, the aggregation pathway of lysozyme shifted from fibrillation to the formation of the small worm-like aggregates with unfolding. The interaction between Cys and lysozyme was observed to be non-covalent, suggesting that the thiophilic interaction between the thiol group on the side chain of Cys and the core sequence of lysozyme significantly contributes to the inhibition of amyloid aggregation. These findings provide a new basis for the design of a biocompatible additive to prevent amyloid fibrillation.

Inhibitors of amyloid fibril formation have been at the centre of intense research efforts for the prevention of amyloidosis. Here, we hypothesise that a specific non-covalent interaction, the thiophilic interaction between the side chain of an aromatic residue in a polypeptide and a sulphur atom of the compound, effectively inhibits amyloid fibril formation. Fluorescence spectroscopy and transmission electron microscopy revealed that sulphur compounds, particularly Cys, inhibit the fibrillisation of amyloid-β 1-40 (Aβ40) and 1-42 (Aβ42). Interestingly, aggregates of Aβ40 and Aβ42 induced by Cys were less cytotoxic than those induced by catechin, which is the most typical inhibitor of amyloid fibril formation. Because the essential amino acid, Cys, is an abundant molecule in the blood and cytosol, our data provide a new basis for the prevention of amyloid-related diseases and the elucidation of the mechanism of these diseases.

No abstract

No abstract