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Nanoparticles in relation to peptide and protein aggregation.

Zaman M, Ahmad E, Qadeer A, Rabbani G, Khan RH - Int J Nanomedicine (2014)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.

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.

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Effect of nanoparticles on nucleation kinetics.Note: The addition of nanoparticles causes an increase in the lag phase and a decrease in the elongation phase.
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f5-ijn-9-899: Effect of nanoparticles on nucleation kinetics.Note: The addition of nanoparticles causes an increase in the lag phase and a decrease in the elongation phase.

Mentions: In order to design an efficient inhibitor, as well as a nanomolecular species that is suitable for this purpose, there is a need to focus on the forces that are responsible for fibrillation. The interactions that are primarily involved in fibril formation are hydrophobic, electrostatic, van der Waals, as well as hydrogen bonding.86 Lee et al87 have demonstrated a three-stage kinetic model for amyloid formation, highlighting the molecular conformational properties that would be needed in order for inhibitors to bind to the nucleus or to other oligomers, so as to reduce their toxic effects. Inhibition by nanoparticles could be done at the nucleation phase (by increasing the lag phase), the polymerization phase (by decreasing the elongation phase), or via diversion of the peptide from the polymerization pathway to reduce the endpoint at equilibrium. Nanoparticles slow down the rate of fibrillation by altering the amount of free monomeric peptides that are present; yet, at the same time, fibril formation could not be prevented.88 Experimental data show that nanoparticles added at the beginning of the kinetic experiment arrest the fibrillation process in lag phase. However, nanoparticles did not show any inhibitory effect when added after the control lag time (Figure 5). This indicates that once critical nuclei are formed, the elongation process is so favorable that the addition of nanoparticles does not have any effect on monomer/oligomer interactions with nanoparticles.88


Nanoparticles in relation to peptide and protein aggregation.

Zaman M, Ahmad E, Qadeer A, Rabbani G, Khan RH - Int J Nanomedicine (2014)

Effect of nanoparticles on nucleation kinetics.Note: The addition of nanoparticles causes an increase in the lag phase and a decrease in the elongation phase.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3928455&req=5

f5-ijn-9-899: Effect of nanoparticles on nucleation kinetics.Note: The addition of nanoparticles causes an increase in the lag phase and a decrease in the elongation phase.
Mentions: In order to design an efficient inhibitor, as well as a nanomolecular species that is suitable for this purpose, there is a need to focus on the forces that are responsible for fibrillation. The interactions that are primarily involved in fibril formation are hydrophobic, electrostatic, van der Waals, as well as hydrogen bonding.86 Lee et al87 have demonstrated a three-stage kinetic model for amyloid formation, highlighting the molecular conformational properties that would be needed in order for inhibitors to bind to the nucleus or to other oligomers, so as to reduce their toxic effects. Inhibition by nanoparticles could be done at the nucleation phase (by increasing the lag phase), the polymerization phase (by decreasing the elongation phase), or via diversion of the peptide from the polymerization pathway to reduce the endpoint at equilibrium. Nanoparticles slow down the rate of fibrillation by altering the amount of free monomeric peptides that are present; yet, at the same time, fibril formation could not be prevented.88 Experimental data show that nanoparticles added at the beginning of the kinetic experiment arrest the fibrillation process in lag phase. However, nanoparticles did not show any inhibitory effect when added after the control lag time (Figure 5). This indicates that once critical nuclei are formed, the elongation process is so favorable that the addition of nanoparticles does not have any effect on monomer/oligomer interactions with nanoparticles.88

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.

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.

Show MeSH
Related in: MedlinePlus