Surface induced collapse of Aβ1-42 with the F19A replacement following adsorption on a single walled carbon nanotube.
Spontaneous adsorption of the Aβ peptide on the surface of a single-walled carbon nanotube, resulting in the prevention of its intrinsic propensity to form collapsed states, could be a plausible means to hinder the peptide's initial nucleation and self-assembly. We report here the effects of sharply reducing both aromatic and hydrophobic character within the peptide's central hydrophobic core on its free and surface behavior. In such an altered peptide, complete surface adsorption is found to induce, rather than prevent, the adsorbed peptide's collapse. The weakened surface interactions of the central hydrophobic core allow its greater translational mobility on the surface, thereby facilitating interactions that lead to compaction. Both the adsorption and the subsequent collapse are accompanied by a loss of surface hydration in the modified peptide. We further find that such a two-step dewetting leads to hydration levels comparable to that obtained after compaction of the free peptide. These insights may be leveraged for designing molecular surfaces for disrupting intrinsic Aβ behavior.
Physical Chemistry Division, CSIR-National Chemical Laboratory, Mr. Homi Bhaba Road, Pune 411008, India.
Asis K
AK
Jana
Neelanjana
N
Sengupta
D000327:Adsorption; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000235:genetics; D009154:Mutation; D037742:Nanotubes, Carbon / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics; D013499:Surface Properties; D013816:Thermodynamics
D016229:Amyloid beta-Peptides; D037742:Nanotubes, Carbon; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)
Adsorption; Amyloid beta peptide; Carbon nanotube; Lateral mobility; Molecular dynamics simulation; Surface induced collapse