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Gallium nanoparticles as novel inhibitors of Aß40 aggregation.
Torres, Kyabeth M; Delgado, Ambar S; Serrano, Erika R; Falcón-Cruz, Nitza V; Meléndez, Anamaris; Ramos, Idalia; Du, Deguo; Oyola, Rolando.
Afiliação
  • Torres KM; University of Puerto Rico-Humacao, Department of Biology, Call Box 860 Humacao 00792 PR USA.
  • Delgado AS; University of Puerto Rico-Humacao, Department of Biology, Call Box 860 Humacao 00792 PR USA.
  • Serrano ER; University of Puerto Rico-Humacao, Department of Chemistry, Call Box 860 Humacao 00792 PR USA rolando.oyola@upr.edu.
  • Falcón-Cruz NV; University of Puerto Rico-Humacao, Department of Chemistry, Call Box 860 Humacao 00792 PR USA rolando.oyola@upr.edu.
  • Meléndez A; University of Puerto Rico-Humacao, Department of Physics & Electronics, Call Box 860 Humacao 00792 PR USA.
  • Ramos I; University of Puerto Rico-Humacao, Department of Physics & Electronics, Call Box 860 Humacao 00792 PR USA.
  • Du D; Florida Atlantic University, Department of Chemistry & Biochemistry Boca Raton 33431 FL USA ddu@fau.edu.
  • Oyola R; University of Puerto Rico-Humacao, Department of Chemistry, Call Box 860 Humacao 00792 PR USA rolando.oyola@upr.edu.
Mater Adv ; 2(16): 5471-5478, 2021 Aug 16.
Article em En | MEDLINE | ID: mdl-34458846
ABSTRACT
Alzheimer's disease (AD) has been consistently related to the formation of senile amyloid plaques mainly composed of amyloid ß (Aß) peptides. The toxicity of Aß aggregates has been indicated to be responsible for AD pathology. One scenario to decrease Aß toxicity is the development of effective inhibitors against Aß amyloid formation. In this study, we investigate the effect of gallium nitride nanoparticles (GaN NPs) as inhibitors of Aß40 amyloid formation using a combination of biophysical approaches. Our results show that the lag phase of Aß40 aggregation kinetics is significantly retarded by GaN NPs in a concentration dependent manner, implying the activity of GaN NPs in interfering with the formation of the crucial nucleus during Aß aggregation. Our results also show that GaN NPs can reduce the amyloid fibril elongation rate in the course of the aggregation kinetics. It is speculated that the high polarization characteristics of GaN NPs may provoke a strong interaction between the particles and Aß40 peptide and in this way decrease self-association of the peptide monomers to form amyloids.

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2021 Tipo de documento: Article