作者: Isaac Fernández-Gómez , Marquiza Sablón-Carrazana , Alberto Bencomo-Martínez , Guadalupe Domínguez , Reyna Lara-Martínez
DOI: 10.3390/MOLECULES23030686
关键词: Amino acid 、 Peptide 、 Cytotoxicity 、 Chemistry 、 Cell biology 、 Proteostasis 、 Drug discovery 、 In silico 、 Protein aggregation 、 Protein folding
摘要: Human islet amyloid peptide (hIAPP1–37) aggregation is an early step in Diabetes Mellitus. We aimed to evaluate a family of pharmaco-chaperones act as modulators that provide dynamic interventions and the multi-target capacity (native state, cytotoxic oligomers, protofilaments fibrils hIAPP1–37) required meet treatment challenges diabetes. used cross-functional approach combines silico vitro biochemical biophysical methods study hIAPP1–37 aggregation-oligomerization process reveal novel potential anti-diabetic drugs. The are oligomerization fibre formation hIAPP1–37. When they interact with amino acid amyloid-like steric zipper zone, inhibit and/or delay pathway by binding stabilizing several structures Moreover, can protect cerebellar granule cells (CGC) from cytotoxicity produced oligomers. modulation proteostasis A–F promising limit onset progression diabetes its comorbidities.