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Nanoparticles in relation to peptide and protein aggregation

Authors Zaman M, Ahmad E, Qadeer A, Rabbani G, Khan RH

Received 7 September 2013

Accepted for publication 30 October 2013

Published 12 February 2014 Volume 2014:9(1) Pages 899—912

DOI https://doi.org/10.2147/IJN.S54171

Checked for plagiarism Yes

Review by Single-blind

Peer reviewer comments 4

Masihuz Zaman, Ejaz Ahmad, Atiyatul Qadeer, Gulam Rabbani, Rizwan Hasan Khan

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.

Keywords: amyloid formation, inducer, inhibitor, nanoparticle, nucleation, toxicity

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