Interaction of Human Resistin with Human Islet Amyloid Polypeptide at Charged Phospholipid Membranes

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 beta-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.

Automated summary

This study presents an X-ray reflectivity investigation on the interaction between recombinant human resistin and fibrillation-prone human islet amyloid polypeptide at anionic phospholipid Langmuir films. The results demonstrate that resistin can inhibit or prevent amyloid-induced lipid membrane rupture, even in the presence of aggregation-promoting negatively charged lipid interfaces. Strong hydrophobic interactions of resistin at the bare buffer-air interface were also found.