Dual-targeted carbon-dot-drugs nanoassemblies for modulating Alzheimer's related amyloid-β aggregation and inhibiting fungal infection
Amyloid aggregation and fungal infection, especially amyloid beta (Aβ) peptide and Candida albicans are considered as two of the crucial pathogenic agents in Alzheimer's disease (AD). In this work, we propose an innovative treatment strategy for AD, targeting at not only Aβ aggregation but also...
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Elsevier
2021-09-01
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| Series: | Materials Today Bio |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590006421000752 |
| _version_ | 1818353046706454528 |
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| author | Chaoren Yan Chaoli Wang Xu Shao Qi Shu Xiaoling Hu Ping Guan Yonggang Teng Yuan Cheng |
| author_facet | Chaoren Yan Chaoli Wang Xu Shao Qi Shu Xiaoling Hu Ping Guan Yonggang Teng Yuan Cheng |
| author_sort | Chaoren Yan |
| collection | DOAJ |
| description | Amyloid aggregation and fungal infection, especially amyloid beta (Aβ) peptide and Candida albicans are considered as two of the crucial pathogenic agents in Alzheimer's disease (AD). In this work, we propose an innovative treatment strategy for AD, targeting at not only Aβ aggregation but also Candida albicans infection. Here, a high-performance nanomaterial, namely gCDs-E, have been prepared by self-assembled of glycosylated carbon dots (gCDs) and epigallocatechin-3-gallate (EGCG). Surprisingly, gCDs-E can not only suppress the fibrillation of Aβ and disaggregate Aβ fibrils, but also effectively inhibit the activity of Candida albicans. More importantly, the prepared gCDs-E can effectively cut down the cytotoxicity of amyloid aggregations, and the cell viability reached to 99.2%. In addition, the capability of the gCDs-E for blood brain barrier (BBB) penetration was also observed using a normal mice model. Above all, the gCDs-E greatly cleaned Aβ deposition and improved memory impairment in APP/PS1 transgenic AD model mice, confirming its potential as therapeutic agent for AD treatment. |
| first_indexed | 2024-12-13T19:03:18Z |
| format | Article |
| id | doaj.art-94aad36350f046099a9215474c69ab91 |
| institution | Directory Open Access Journal |
| issn | 2590-0064 |
| language | English |
| last_indexed | 2024-12-13T19:03:18Z |
| publishDate | 2021-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Materials Today Bio |
| spelling | doaj.art-94aad36350f046099a9215474c69ab912022-12-21T23:34:38ZengElsevierMaterials Today Bio2590-00642021-09-0112100167Dual-targeted carbon-dot-drugs nanoassemblies for modulating Alzheimer's related amyloid-β aggregation and inhibiting fungal infectionChaoren Yan0Chaoli Wang1Xu Shao2Qi Shu3Xiaoling Hu4Ping Guan5Yonggang Teng6Yuan Cheng7Department of Chemistry, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi'an, 710072, PR ChinaDepartment of Pharmaceutical Analysis, School of Pharmacy, Air Force Medical University, Xi'an, 710032, PR ChinaDepartment of Chemistry, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi'an, 710072, PR ChinaDepartment of Chemistry, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi'an, 710072, PR ChinaDepartment of Chemistry, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi'an, 710072, PR China; Corresponding author.Department of Chemistry, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi'an, 710072, PR China; Corresponding author.Department of Thoracic Surgery, The Second Affiliated Hospital of Air Force Medical University, Xi'an, ChinaMonash Suzhou Research Institute, Suzhou, 215123, PR China; Department of Mechanical and Aerospace Engineering, Monash University, Clayton Victoria, 3800, Melbourne, Australia; Corresponding author. Monash Suzhou Research Institute, Suzhou, 215123, PR China.Amyloid aggregation and fungal infection, especially amyloid beta (Aβ) peptide and Candida albicans are considered as two of the crucial pathogenic agents in Alzheimer's disease (AD). In this work, we propose an innovative treatment strategy for AD, targeting at not only Aβ aggregation but also Candida albicans infection. Here, a high-performance nanomaterial, namely gCDs-E, have been prepared by self-assembled of glycosylated carbon dots (gCDs) and epigallocatechin-3-gallate (EGCG). Surprisingly, gCDs-E can not only suppress the fibrillation of Aβ and disaggregate Aβ fibrils, but also effectively inhibit the activity of Candida albicans. More importantly, the prepared gCDs-E can effectively cut down the cytotoxicity of amyloid aggregations, and the cell viability reached to 99.2%. In addition, the capability of the gCDs-E for blood brain barrier (BBB) penetration was also observed using a normal mice model. Above all, the gCDs-E greatly cleaned Aβ deposition and improved memory impairment in APP/PS1 transgenic AD model mice, confirming its potential as therapeutic agent for AD treatment.http://www.sciencedirect.com/science/article/pii/S2590006421000752Glycosylated carbon dotsEpigallocatechin-3-gallateAmyloid-βpeptideCandida albicansAlzheimer's disease |
| spellingShingle | Chaoren Yan Chaoli Wang Xu Shao Qi Shu Xiaoling Hu Ping Guan Yonggang Teng Yuan Cheng Dual-targeted carbon-dot-drugs nanoassemblies for modulating Alzheimer's related amyloid-β aggregation and inhibiting fungal infection Materials Today Bio Glycosylated carbon dots Epigallocatechin-3-gallate Amyloid-βpeptide Candida albicans Alzheimer's disease |
| title | Dual-targeted carbon-dot-drugs nanoassemblies for modulating Alzheimer's related amyloid-β aggregation and inhibiting fungal infection |
| title_full | Dual-targeted carbon-dot-drugs nanoassemblies for modulating Alzheimer's related amyloid-β aggregation and inhibiting fungal infection |
| title_fullStr | Dual-targeted carbon-dot-drugs nanoassemblies for modulating Alzheimer's related amyloid-β aggregation and inhibiting fungal infection |
| title_full_unstemmed | Dual-targeted carbon-dot-drugs nanoassemblies for modulating Alzheimer's related amyloid-β aggregation and inhibiting fungal infection |
| title_short | Dual-targeted carbon-dot-drugs nanoassemblies for modulating Alzheimer's related amyloid-β aggregation and inhibiting fungal infection |
| title_sort | dual targeted carbon dot drugs nanoassemblies for modulating alzheimer s related amyloid β aggregation and inhibiting fungal infection |
| topic | Glycosylated carbon dots Epigallocatechin-3-gallate Amyloid-βpeptide Candida albicans Alzheimer's disease |
| url | http://www.sciencedirect.com/science/article/pii/S2590006421000752 |
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