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- W4283025260 abstract "An X-ray reflectivity study on the interaction of recombinant human resistin (hRes) with fibrillation-prone human islet amyloid polypeptide (hIAPP) at anionic phospholipid Langmuir films as model membranes is presented. Aggregation and amyloid formation of hIAPP is considered the main mechanism of pancreatic β-cell loss in patients with type 2 diabetes mellitus. Resistin shows a chaperone-like ability, but also tends to form aggregates by itself. Resistin and hIAPP cross multiply metabolism pathways. In this study, we researched the potential protective effects of resistin against hIAPP-induced lipid membrane rupture. The results demonstrate that resistin can inhibit or prevent hIAPP adsorption even in the presence of aggregation-promoting negatively charged lipid interfaces. Moreover, we found strong hydrophobic interactions of resistin at the bare buffer-air interface." @default.
- W4283025260 created "2022-06-18" @default.
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- W4283025260 date "2022-06-16" @default.
- W4283025260 modified "2023-09-30" @default.
- W4283025260 title "Interaction of Human Resistin with Human Islet Amyloid Polypeptide at Charged Phospholipid Membranes" @default.
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- W4283025260 doi "https://doi.org/10.1021/acsomega.2c01363" @default.
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