1. The synergistic effect between KLVFF and self-assembly chaperones on both disaggregation of beta-amyloid fibrils and reducing consequent toxicity
- Author
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Huiru Yang, Jiafu Long, Linqi Shi, Aoting Qu, Ang Li, Fan Huang, and Hao Zhou
- Subjects
0301 basic medicine ,Amyloid ,Surface Properties ,Peptide ,Fibril ,Protein Aggregation, Pathological ,Catalysis ,Protein Aggregates ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Materials Chemistry ,Particle Size ,Micelles ,chemistry.chemical_classification ,Amyloid beta-Peptides ,biology ,Metals and Alloys ,Drug Synergism ,General Chemistry ,Amyloid fibril ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,030104 developmental biology ,Monomer ,chemistry ,Biochemistry ,Chaperone (protein) ,Toxicity ,Ceramics and Composites ,biology.protein ,Biophysics ,Self-assembly ,Hydrophobic and Hydrophilic Interactions ,Oligopeptides ,030217 neurology & neurosurgery ,Molecular Chaperones - Abstract
By combining KLVFF peptide and self-assembly chaperone we fabricate a new system to achieve the synchronization between Aβ fibril disaggregation and reducing toxicity of Aβ fragments (monomers or oligomers) that consequently formed. When the KLVFF peptides disaggregate fibrils into fragments, the hydrophobic domains of self-assembly chaperones promptly bind them at the same time. This binding blocks the re-aggregation of the fragments and their interaction with cells, and hence reduces the toxicity of these dangerous fragments.
- Published
- 2017