The curvature of gold nanoparticles influences the exposure of amyloid-β and modulates its aggregation process

Inhibition Of Tau Protein Aggregation By a Chaperone-like β-Boswellic Acid Conjugated To Gold Nanoparticles

“… 56 , 66 − 70 Overall, it can be deduced that NP displays a dual manner that interferes with the protein amyloid formation. In our study, the highest efficacy of U-G-BA in the inhibition of tau protein aggregation might be due to the larger diameter of U-G, and possibly higher amounts of the BA carried on U-G compared to C-G. 71 The CD spectra data of tau fibrillation in the presence of BA, GNP, and GNP-BA confirmed the ThT fluorescence results ( Figure S1 ). 54 These results are further supported by our AFM studies on C-G-BA ( Figure 4 d) and U-G-BA ( Figure 5 d).…”

Influencing factors and characterization methods of nanoparticles regulating amyloid aggregation

“…149 In the SERS spectrogram of NPs for the modulation of Ab1-42, the typical signals and characteristic peaks were used to determine the b-sheet conformation of the aggregates and analyze the residual amino acid residues on the surface of the NPs, by which their interactions can be studied, and thus provide information about the process and aggregation results. 62 The positive band at 1227 cm À1 was enhanced as the peptide concentration increases, which can be explained by the structural transition from the a-helix and disordered structure to the b-sheet and b-turn structure (Fig. 4A).…”

“…61 In contrast, rarely, some NPs exhibit no effect on amyloid aggregation due to the weak interaction between the NPs and peptides being unable to produce an affinity for amyloid peptides. 62 The nucleation and growth process of amyloid peptide or protein aggregate fibrillation follows a kinetic process, which may reveal the possible mechanism of amyloid aggregation in terms of classical nucleation theory, conformational transformation, and secondary nucleation in multiple ways. NPs are used to regulate amyloid aggregation, because the surface effects and the results of biological coating affect the different kinetic stages of aggregation and fibrillation.…”

“…2A). 62 The spherical NP model fails to capture the trajectory of the amyloid peptides in their possible orientations on the surface. 73 It can be concluded that NPs with small size and greater curvature show better suppression.…”

“…61 In contrast, rarely, some NPs exhibit no effect on amyloid aggregation due to the weak interaction between the NPs and peptides being unable to produce an affinity for amyloid peptides. 62…”