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Atomic force microscopy based nanoassay: a new method to study α-Synuclein-dopamine bioaffinity interactions
- Source :
- Scientific Reports, Scientific Reports, 4
- Publication Year :
- 2014
- Publisher :
- Nature Publishing Group, 2014.
-
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.<br />Scientific Reports, 4<br />ISSN:2045-2322
- Subjects :
- Pathology
medicine.medical_specialty
Computer science
Dopamine
Metal Nanoparticles
Plasma protein binding
Multidisciplinary
alpha synuclein
dopamine
gold
metal nanoparticle
protein binding
adsorption
atomic force microscopy
binding site
chemistry
nanotechnology
procedures
protein analysis
sensitivity and specificity
Adsorption
alpha-Synuclein
Binding Sites
Gold
Microscopy, Atomic Force
Nanotechnology
Protein Binding
Protein Interaction Mapping
Sensitivity and Specificity
Intrinsically disordered proteins
Article
Supramolecular assembly
Settore FIS/03 - Fisica della Materia
chemistry.chemical_compound
medicine
Applications of AFM
Binding site
Nanoscopic scale
Alpha-synuclein
Microscopy
Atomic Force
Small molecule
Characterization (materials science)
Dissociation constant
Biophysics
medicine.drug
Subjects
Details
- Language :
- English
- ISSN :
- 20452322
- Volume :
- 4
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....724c279cda1de708449a4d9552db38c9