Bleomycin modulates amyloid aggregation in β-amyloid and hIAPP
Anchala Kumari, Ritika Sharma, Nidhi Shrivastava, Pallavi Somvanshi, Abhinav Grover
Abstract
amyloid aggregation assays was obtained wherein the fibrillar load was decreased for the BLM-treated Aβ and hIAPP peptides in comparison to controls. For the first time, this study shows that BLM is a dual inhibitor of Aβ and hIAPP amyloid aggregation. In the future, the conformational optimization and processing of BLM may help develop various efficient sequence-dependent inhibitors against amyloid aggregation in various amyloid peptides.
Topics & Concepts
Amyloid (mycology)ChemistryAmyloid diseasePeptideBiochemistryBiophysicsFibrilP3 peptideAmyloidosisAmyloid fibrilAmyloid βAmyloid precursor proteinBiologyAlzheimer's diseaseMedicineDiseasePathologyInorganic chemistryAlzheimer's disease research and treatmentsDrug Transport and Resistance MechanismsComputational Drug Discovery Methods