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Int J Biol Macromol. 2017 Jan;94(Pt A):386-395. doi: 10.1016/j.ijbiomac.2016.10.024. Epub 2016 Oct 13.

Nanoparticles-protein interaction: Role in protein aggregation and clinical implications.

Author information

1
Genes and Proteins Lab, Department of Biotechnology, Jamia Millia Islamia, New Delhi, 110025, India.
2
Genes and Proteins Lab, Department of Biotechnology, Jamia Millia Islamia, New Delhi, 110025, India. Electronic address: amu.jmi@rediffmail.com.

Abstract

This review helps to understand protein misfolding events, which results in protein aggregation, and hence to related neurodegenerative diseases. Many chaperones and folding factors are found inside the cell system for the proper folding of protein. If protein gets misfolded, it may accumulate in cells and can lead to several fatal diseases. In some cases, misfolded proteins aggregated in form of loop-sheet polymer and amyloid fibril when they escape the degradation process and leads to neurodegenerative disorders. Nanoparticles (NPs) are nano-sized materials, can be formulated by using organic molecules such as gelatin, chitosan, inorganic molecules, metals such as iron, gold, silver, etc. NPs unite with proteins and form a dynamic nanoparticle-protein (NP-P) corona. Conformational changes may be induced in adsorbed protein by this NP-P corona which might change overall bio-reactivity of NP. They can influence correct folding of unfolded or misfolded protein and prevent their aggregation which may be helpful in the cure of neurodegenerative disorders. Due to high area:size ratio, NPs have higher advantages over bulk materials. Hence, the effect of NPs on the proper protein folding opens new gateways to produce a biologically active three dimensional biomolecule.

KEYWORDS:

Adsorption; Circular dichroism; Cyclodextrins; Nanoparticles; Nanospheres; Nanotechnology; Protein aggregation; Protein binding; Protein folding/refolding; Protein structure

PMID:
27746352
DOI:
10.1016/j.ijbiomac.2016.10.024
[Indexed for MEDLINE]

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