Publication | Closed Access
Ruthenium complexes as novel inhibitors of human islet amyloid polypeptide fibril formation
37
Citations
38
References
2013
Year
Proteinlipid InteractionChemical BiologyType IiInsulin SignalingFibril FormationProtein MisfoldingHuman Islet AmyloidBiochemistryRuthenium ComplexesBiochemical InteractionBiopolymersPharmacologyBiomolecular Engineeringβ-Sheet ComponentsNatural SciencesDiabetesPeptide TherapeuticProtein EngineeringMedicineDrug Discovery
Human islet amyloid polypeptide (hIAPP) can be linked to the pathology of type II diabetes. In this study, aromatic ring-containing Ru complexes were found to effectively inhibit the fibril formation of hIAPP and promote the disaggregation of formed fibrils by remarkably changing the β-sheet components.
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