Regulation of heteronuclear Pt–Ru complexes on the fibril formation and cytotoxicity of human islet amyloid polypeptide

Exploration of Isoquinoline Alkaloids as Potential Inhibitors against Human Islet Amyloid Polypeptide

“…Meanwhile, amylin can accumulate in the heart, brain, kidney, and other important organs, thereby causing more serious complications. , Many recent studies have focused on hIAPP to inhibit its aggregation and find effective drug candidates for the prevention and treatment of T2DM. Current hIAPP inhibitors include oligopeptides, aromatic molecules, metal complexes, natural products, polymers, and nanoparticles. − Multifunctional nanocomposites with certain structural and physicochemical properties are increasingly used to alleviate amyloidosis in vitro and in vivo . The generation-3 OH-terminated poly (amidoamine) dendrimer can effectively prevent the aggregation of hIAPP and reduce peptide toxicity in different pancreatic cell lines and mouse islets .…”

Platinum(II) O,S Complexes Inhibit the Aggregation of Amyloid Model Systems

“…The aggregation of the peptide spanning residues 106–126 of Prion Protein (PrP 106–126 ) can be inhibited by its interaction with the Ru(III) complex NAMI-A or by its analogues [38]. Similarly, it has been demonstrated that the amyloid aggregation of human islet amyloid polypeptide (hIAPP) can be inhibited by metal complexes containing homo-dinuclear Ru [39,40] and hetero-multinuclear Pt-Ru systems [41]. In these cases, the binding of metal complexes to hIAPP produces a spontaneous, enthalpy-driven process, due to both hydrophobic interactions and metal coordination.…”

Human islet amyloid polypeptide: A therapeutic target for the management of type 2 diabetes mellitus

“…Using thioflavin T fluorescence assays and transmission electron microscopic analysis of INS-1E cells, a previous study has shown that gold-sulfur complexes such as dichloro-diethyl-dithiocarbamate and dichloro-pyrrolidine-dithiocarbamate gold complexes inhibit hIAPP fibrillation in vitro [ 247 ]. Likewise, heme [ 248 ], methionine-ruthenium complex [ 249 ], and platinum-ruthenium complex [ 250 ] exert a strong inhibitory effect on hIAPP aggregation. All these agents have shown their inhibitory activity in vitro , and it would be interesting to explore their effects in vivo in the future ( Table S5 ) [ [243] , [244] , [245] , [246] , [247] , [248] , [249] , [250] , [251] , [252] ].…”

“…Likewise, heme [ 248 ], methionine-ruthenium complex [ 249 ], and platinum-ruthenium complex [ 250 ] exert a strong inhibitory effect on hIAPP aggregation. All these agents have shown their inhibitory activity in vitro , and it would be interesting to explore their effects in vivo in the future ( Table S5 ) [ [243] , [244] , [245] , [246] , [247] , [248] , [249] , [250] , [251] , [252] ].…”