Human Serum Albumin Aggregation and its Modulation Using Nanoparticles: A Review

Santhosh Paramasivam, Kavita Kundal, Nandini Sarkar

Research output: Contribution to journalReview articlepeer-review

3 Scopus citations

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.

Original languageEnglish
Pages (from-to)11-21
Number of pages11
JournalProtein and Peptide Letters
Volume29
Issue number1
DOIs
StatePublished - 1 Jan 2022
Externally publishedYes

Keywords

  • Human serum albumin
  • amyloids
  • biodegradable
  • nanoparticles
  • protein aggregation
  • protein misfolding

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

Fingerprint

Dive into the research topics of 'Human Serum Albumin Aggregation and its Modulation Using Nanoparticles: A Review'. Together they form a unique fingerprint.

Cite this