volume 30 issue 2 pages 139-151

Clay-Polymer Nanocomposites Mediated Inhibition of Protein Aggregation: Possible Role in the Prevention of Proteinopathies

Publication typeJournal Article
Publication date2025-03-01
scimago Q3
wos Q4
SJR0.338
CiteScore2.4
Impact factor1.1
ISSN09298665, 18755305
Biochemistry
General Medicine
Structural Biology
Abstract
Background:

The transformation of proteins from their native conformation into highly ordered fibrillar structures due to their misfolding and aggregation under particular conditions are described as beta-sheet enriched amyloid fibrils. The accumulation of these fibrils in different body parts is the major cause of several neurological and non-neurological conditions (proteinopathies).

Objectives:

To prevent these proteinopathies, inhibition of protein aggregation is considered a promising strategy. Therefore, in this study, we synthesized montmorillonite (MMT) based poly- orthophenylenediamine (PoPD) nanocomposites (NCs) and characterized their size and morphology due to their remarkable biological properties. Further, the effect of these nanocomposites on inhibition of fibril formation was assessed.

Methods:

These nanocomposites were evaluated for their anti-amyloidogenic potential on two model proteins of amyloidopathies, i.e., human lysozyme and human serum albumin (HL & HSA), by using several biophysical methods, such as Thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) fluorescence, congo red dye binding assay (CR). Secondary structural content was evaluated by Circular dichroism (CD) spectroscopy.

Results:

Results demonstrated that synthesized nanocomposites significantly inhibited fibril formation in dose-dependent manner that corresponds to their ability to arrest fibrillation. It is suggested that they may adsorb proteins to protect them against aggregation when they are subjected to aggregating conditions.

Conclusion:

This study offers an opportunity to understand the mechanism of inhibition of fibril formation by nanocomposites, showing that they inhibit amyloid formation and amyloid diseases. Thus, the study concludes that these nanocomposites are promising candidates as therapeutic molecules for proteinopathies and are envisaged to enrich the area of personalized medicine, augmenting the human healthcare system.

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Parveen R. et al. Clay-Polymer Nanocomposites Mediated Inhibition of Protein Aggregation: Possible Role in the Prevention of Proteinopathies // Protein and Peptide Letters. 2025. Vol. 30. No. 2. pp. 139-151.
GOST all authors (up to 50) Copy
Parveen R., Ali S., Fatima S. Clay-Polymer Nanocomposites Mediated Inhibition of Protein Aggregation: Possible Role in the Prevention of Proteinopathies // Protein and Peptide Letters. 2025. Vol. 30. No. 2. pp. 139-151.
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TY - JOUR
DO - 10.2174/0109298665274059231002071951
UR - https://www.eurekaselect.com/221726/article
TI - Clay-Polymer Nanocomposites Mediated Inhibition of Protein Aggregation: Possible Role in the Prevention of Proteinopathies
T2 - Protein and Peptide Letters
AU - Parveen, Romana
AU - Ali, Sher
AU - Fatima, Sadaf
PY - 2025
DA - 2025/03/01
PB - Bentham Science Publishers Ltd.
SP - 139-151
IS - 2
VL - 30
PMID - 37855298
SN - 0929-8665
SN - 1875-5305
ER -
BibTex |
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BibTex (up to 50 authors) Copy
@article{2025_Parveen,
author = {Romana Parveen and Sher Ali and Sadaf Fatima},
title = {Clay-Polymer Nanocomposites Mediated Inhibition of Protein Aggregation: Possible Role in the Prevention of Proteinopathies},
journal = {Protein and Peptide Letters},
year = {2025},
volume = {30},
publisher = {Bentham Science Publishers Ltd.},
month = {mar},
url = {https://www.eurekaselect.com/221726/article},
number = {2},
pages = {139--151},
doi = {10.2174/0109298665274059231002071951}
}
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Parveen, Romana, et al. “Clay-Polymer Nanocomposites Mediated Inhibition of Protein Aggregation: Possible Role in the Prevention of Proteinopathies.” Protein and Peptide Letters, vol. 30, no. 2, Mar. 2025, pp. 139-151. https://www.eurekaselect.com/221726/article.