Atomic force microscopy based nanoassay: A new method to study α-Synuclein-dopamine bioaffinity interactions

Stefania Corvaglia, Barbara Sanavio, Rolando P. Hong Enriquez, Barbara Sorce, Alessandro Bosco, Denis Scaini, Stefania Sabella, Pier Paolo Pompa, Giacinto Scoles, Loredana Casalis

Research output: Contribution to journalArticlepeer-review

Abstract

Intrinsically Disordered Proteins (IDPs) are characterized by the lack of well-defined 3-D structure and show high conformational plasticity. For this reason, they are a strong challenge for the traditional characterization of structure, supramolecular assembly and biorecognition phenomena. We show here how the fine tuning of protein orientation on a surface turns useful in the reliable testing of biorecognition interactions of IDPs, in particular α-Synuclein. We exploited atomic force microscopy (AFM) for the selective, nanoscale confinement of α-Synuclein on gold to study the early stages of α-Synuclein aggregation and the effect of small molecules, like dopamine, on the aggregation process. Capitalizing on the high sensitivity of AFM topographic height measurements we determined, for the first time in the literature, the dissociation constant of dopamine-α-Synuclein adducts.

Original languageEnglish
Article number5366
JournalScientific Reports
Volume4
DOIs
Publication statusPublished - Jun 20 2014

ASJC Scopus subject areas

  • General

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