Abstract
Some misfolded proteins, e.g., immunoglobulin monoclonal free light chains (FLC), tend to form fibrils. Protein deposits in tissue may lead to amyloidosis and dysfunction of different organs. There is currently no technique allowing for the identification of FLC that are prone to aggregate. The development of such a method would enable the early selection of patients at high risk of developing amyloidosis. The aim of this study was to investigate whether silver nanoparticles (AgNPs) could be a useful tool to study the process of aggregation of FLC and their susceptibility to form the protein deposits. Mixtures of AgNPs and urine samples from patients with multiple myeloma were prepared. To evaluate the aggregation process of nanoparticles coated with proteins, UV-visible spectroscopy, transmission electron microscopy, and the original laser light scattering method were used. It has been shown that some clones of FLC spontaneously triggered aggregation of the nanoparticles, while in the presence of others, the nanoparticle solution became hyperstable. This is probably due to the structure of the chains themselves, unique protein-AgNPs interactions and perhaps correlates with the tendency of some FLC clones to form deposits. Nanoparticle technology has proven to be helpful in identifying clones of immunoglobulin FLC that tend to aggregate.
Highlights
Immunoglobulin monoclonal free light chains (FLC) are involved in several protein deposition diseases, e.g., light chain amyloidosis (AL amyloidosis) and light chain deposition disease
In AL amyloidosis, FLC form characteristic amyloid fibrils which are deposited in tissues, while in light chain deposition disease, protein deposits are amorphous [1]
The aim of this study was to investigate whether silver nanoparticles can be a useful tool for identifying FLC clones that tend to interact and aggregate
Summary
Immunoglobulin monoclonal free light chains (FLC) are involved in several protein deposition diseases, e.g., light chain amyloidosis (AL amyloidosis) and light chain deposition disease. Amyloidosis is a group of protein conformational diseases caused by misfolding, aggregation and deposition of different proteins, mainly in the extracellular spaces of organs and tissues. These protein deposits have characteristic form of insoluble, non-branching, rigid fibrils [2]. Amyloid fibrils have a diameter of 7–13 nm and similar core structure consisting of, mainly, anti-parallel β-strands which form sheets [3]. These fibrils are characterized by their capacity to bind the dye Congo red and show apple-green birefringence under polarized light [4]. There have been more 30 different proteins identified so far as a possible cause of amyloidosis, and, with the use of mass spectrometry-based proteomic analysis, the number of amyloid precursors is still increasing [2]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
