Abstract
Introduction: Proteinopathies are a group of diseases where the protein structure has been altered. These alterations are linked to the production of amyloids, which are persistent, organized clumps of protein molecules through inter-molecular interactions. Several disorders, including Alzheimer's and Parkinson's, have been related to the presence of amyloids. Highly ordered beta sheets or beta folds are characteristic of amyloids; these structures can further self- assemble into stable fibrils.
Methods: Protein aggregation is caused by a wide variety of environmental and experimental factors, including mutations, high pH, high temperature, and chemical modification. Despite several efforts, a cure for amyloidosis has yet to be found. Due to its advantageous semi-conducting characteristics, unique optical features, high surface area-to-volume ratio, biocompatibility, etc., carbon quantum dots (CQDs) have lately emerged as key instruments for a wide range of biomedical applications. To this end, we have investigated the effect of CQDs with a carboxyl group on their surface (CQD-CA) on the in vitro amyloidogenesis of hen egg white lysozyme (HEWL).
Results: By generating a stable compound that is resistant to fibrillation, our findings show that CQD-CA can suppress amyloid and disaggregate HEWL. In addition, CQD-CA caused the creation of non-toxic spherical aggregates, which generated much less reactive oxygen species (ROS).
Conclusion: Overall, our results show that more research into amyloidosis treatments, including surface functionalized CQDs, is warranted.
Graphical Abstract
[http://dx.doi.org/10.1039/C4CP05563B] [PMID: 25719972]
[http://dx.doi.org/10.1016/j.cell.2010.11.050] [PMID: 21215370]
[http://dx.doi.org/10.1007/s10930-017-9705-2] [PMID: 28299593]
[http://dx.doi.org/10.1016/j.electacta.2018.11.167]
[http://dx.doi.org/10.1038/srep31100] [PMID: 27492748]
[http://dx.doi.org/10.1039/c2ra00030j]
[http://dx.doi.org/10.5935/0103-5053.20150094]
[http://dx.doi.org/10.1016/j.apsusc.2016.08.106]
[http://dx.doi.org/10.1002/chem.201304869] [PMID: 24623706]
[http://dx.doi.org/10.1016/j.biomaterials.2012.01.052] [PMID: 22341214]
[http://dx.doi.org/10.1038/s41598-017-04073-1] [PMID: 28667269]
[http://dx.doi.org/10.1039/c2cc33844k] [PMID: 22911246]
[http://dx.doi.org/10.1002/ejic.201000622]
[http://dx.doi.org/10.1002/chem.201203641] [PMID: 23322649]
[http://dx.doi.org/10.1016/j.snb.2014.02.053]
[http://dx.doi.org/10.1039/C5AN00454C] [PMID: 25927267]
[http://dx.doi.org/10.1016/j.snb.2016.11.109]
[http://dx.doi.org/10.1016/j.matlet.2011.08.081]
[http://dx.doi.org/10.1016/j.carbon.2013.07.095]
[http://dx.doi.org/10.1166/mat.2016.1289]
[http://dx.doi.org/10.2174/157016410791330516]
[http://dx.doi.org/10.1039/D0NA00870B] [PMID: 36133854]
[http://dx.doi.org/10.1021/cm504572b]
[http://dx.doi.org/10.1039/C6TB00976J] [PMID: 32263748]
[http://dx.doi.org/10.1016/j.colsurfb.2019.01.033] [PMID: 30684903]
[http://dx.doi.org/10.3390/nano11092242] [PMID: 34578556]
[PMID: 24611007]
[http://dx.doi.org/10.1016/j.bpc.2021.106714] [PMID: 34749221]
[http://dx.doi.org/10.1016/j.colsurfb.2018.03.010] [PMID: 29550545]
[http://dx.doi.org/10.1080/19336896.2020.1720487] [PMID: 32008441]
[http://dx.doi.org/10.1016/j.bbagen.2011.01.007] [PMID: 21276838]
[http://dx.doi.org/10.1021/jp9115996] [PMID: 20148537]
[http://dx.doi.org/10.1155/2013/349542] [PMID: 23984347]
[http://dx.doi.org/10.1016/j.ijbiomac.2019.12.267] [PMID: 31923519]
[http://dx.doi.org/10.1021/acsami.7b03816] [PMID: 28613069]
[http://dx.doi.org/10.1155/2012/630425]
[http://dx.doi.org/10.1021/acssuschemeng.1c08638]
[http://dx.doi.org/10.1002/bip.20853] [PMID: 17896349]
[http://dx.doi.org/10.1039/c2md20236k]
[http://dx.doi.org/10.1016/j.bbamem.2013.04.012]
[http://dx.doi.org/10.1093/oso/9780199636198.003.0012]
[http://dx.doi.org/10.1073/pnas.260502597] [PMID: 11114199]
[http://dx.doi.org/10.1152/physrev.00026.2013] [PMID: 24987008]
[http://dx.doi.org/10.1016/j.compositesb.2021.109364]