Nanoparticles in relation to peptide and protein aggregation

Abstract

Over the past two decades, there has been considerable research interest in the use of nanoparticles in the study of protein and peptide aggregation, and of amyloid-related diseases. The influence of nanoparticles on amyloid formation yields great interest due to its small size and high surface area-to-volume ratio. Targeting nucleation kinetics by nanoparticles is one of the most searched for ways to control or induce this phenomenon. The observed effect of nanoparticles on the nucleation phase is determined by particle composition, as well as the amount and nature of the particle’s surface. Various thermodynamic parameters influence the interaction of proteins and nanoparticles in the solution, and regulate the protein assembly into fibrils, as well as the disaggregation of preformed fibrils. Metals, organic particles, inorganic particles, amino acids, peptides, proteins, and so on are more suitable candidates for nanoparticle formulation. In the present review, we attempt to explore the effects of nanoparticles on protein and peptide fibrillation processes from both perspectives (ie, as inducers and inhibitors on nucleation kinetics and in the disaggregation of preformed fibrils). Their formulation and characterization by different techniques have been also addressed, along with their toxicological effects, both in vivo and in vitro.

Graphene oxide inhibits hIAPP amyloid fibrillation and toxicity in insulin-producing NIT-1 cells

“…The effects of nanoparticles on protein aggregation may vary, depending on the physicochemical nature of the nanoparticles and the protein in question 18,19 . Past studies showed that GO nanosheets exerted an inhibitory effect on the aggregation of amyloid-β 22 .…”

A Comprehensive Spectroscopic and Computational Investigation to Probe the Interaction of Antineoplastic Drug Nordihydroguaiaretic Acid with Serum Albumins

“…Fig 8A and 8B represents the far-UV CD spectra of HSA and BSA at 1:0, 1:5 and 1:10 protein to NDGA molar ratio. In the absence of NDGA, HSA and BSA exhibits two characteristic peak which are around at 222 nm (n→pi* transition) and 208 nm (pi→pi* transition), a characteristic of α-helix [ 52 , 53 ]. The spectra in the Fig 8A and 8B depicts that NDGA interaction with HSA (& BSA) led to a change in secondary structure of albumin resulting into the increment in helical content of protein.…”

Preparation of Nano-Particles and Their Applications in Adsorption

“…These applications encompass them to be used in electronic, drug delivery, optical, mechanics, catalysis, bio-encapsulation and wastewater treatment especially adsorption [4][5][6][7][8][9][10][11][12][13][14][15]. Besides all these properties, nano-particles have some toxic effects for aquatic and human health.…”