Title:Human Serum Albumin Aggregation and its Modulation Using Nanoparticles: A Review
Volume: 29
Issue: 1
Author(s): Santhosh Paramasivam, Kavita Kundal and Nandini Sarkar*
Affiliation:
- Department of Biotechnology and Medical Engineering, National Institute of Technology Rourkela, Odisha, India
Keywords:
Human serum albumin, protein aggregation, nanoparticles, amyloids, protein misfolding, biodegradable.
Abstract: Amyloid fibrils are highly stable protein fibrillar aggregates believed to be involved in
various neurodegenerative diseases, which include Alzheimer’s disease, Parkinson’s disease, and
prion diseases. Inhibiting the aggregation process is a potential strategy to prevent diseases caused
by amyloid formation. In this regard, nanoparticles have emerged as promising candidates owing
to their unique physical/chemical properties of small size, large surface area, biocompatibility,
biodegradability, non-toxicity, and ease of functionalization. Human Serum Albumin (HSA) is a
soluble multidomain monomeric protein that interacts with various ligands and hormones, aiding in
their transport, distribution, metabolism in the circulatory system, and also plays a vital role in extracellular
fluid volume stabilization. Under certain in vitro conditions, HSA has been reported to
undergo conformational changes leading to fibril formation and hence acts as a suitable model for
studying amyloidogenesis. In this review, we have explored the effects of various nanoparticles on
HSA aggregation and their mechanism of action. The study will throw light on the mechanistic details
of nanoparticle-mediated amyloid modulation, which will help in the development of effective
therapeutics against amyloidosis.