Cargando…
Tyrosine carbon dots inhibit fibrillation and toxicity of the human islet amyloid polypeptide
Misfolding and aggregation of the human islet amyloid polypeptide (hIAPP) are believed to play key roles in the pathophysiology of type-II diabetes. Here, we demonstrate that carbon dots (C-dots) prepared from the amino acid tyrosine inhibit fibrillation of hIAPP, reduce hIAPP-induced cell toxicity...
Autores principales: | Bloch, Daniel Nir, Ben Zichri, Shani, Kolusheva, Sofiya, Jelinek, Raz |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
RSC
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9419576/ https://www.ncbi.nlm.nih.gov/pubmed/36133854 http://dx.doi.org/10.1039/d0na00870b |
Ejemplares similares
-
Scavenging neurotoxic aldehydes using lysine carbon dots
por: Bloch, Daniel Nir, et al.
Publicado: (2023) -
Influence of Aluminium and EGCG on Fibrillation and Aggregation of Human Islet Amyloid Polypeptide
por: Xu, Zhi-Xue, et al.
Publicado: (2016) -
Lipid accelerating the fibril of islet amyloid polypeptide aggravated the pancreatic islet injury in vitro and in vivo
por: Mo, Xiao-Dan, et al.
Publicado: (2018) -
Star Polymers Reduce Islet Amyloid Polypeptide Toxicity
via Accelerated Amyloid Aggregation
por: Pilkington, Emily H., et al.
Publicado: (2017) -
Disaggregation of Islet Amyloid Polypeptide Fibrils as a Potential Anti-Fibrillation Mechanism of Tetrapeptide TNGQ
por: Abioye, Raliat O., et al.
Publicado: (2022)