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Inhibition of toxic metal-alpha synuclein interactions by human serum albumin

Karla Martinez Pomier, Rashik Ahmed, Jinfeng Huang, Giuseppe Melacini

2024Chemical Science15 citationsDOIOpen Access PDF

Abstract

the N-terminus, Tyr 39 and the majority of the C-terminus. Our study not only unveils the effect of fatty acid binding and age-related posttranslational modifications, such as glycation, on the neuroprotective mechanisms of HSA, but also highlights the potential of αSyn as a viable NMR-based sensor to investigate HSA-metal interactions.

Topics & Concepts

SynucleinopathiesAlpha-synucleinHuman serum albuminAlbuminChemistrySerum albuminPlasma protein bindingAlpha (finance)Parkinson's diseaseBiochemistryPharmacologyDiseaseMedicineInternal medicineConstruct validityPatient satisfactionNursingParkinson's Disease Mechanisms and TreatmentsProtein Interaction Studies and Fluorescence AnalysisAlzheimer's disease research and treatments
Inhibition of toxic metal-alpha synuclein interactions by human serum albumin | Litcius