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Article
A kinetic ensemble of the Alzheimer’s Aβ peptide
The conformational and thermodynamic properties of disordered proteins are commonly described in terms of structural ensembles and free energy landscapes. To provide information on the transition rates between...
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Article
Open AccessA rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer’s disease
Bicyclic peptides have great therapeutic potential since they can bridge the gap between small molecules and antibodies by combining a low molecular weight of about 2 kDa with an antibody-like binding specific...
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Article
Open AccessTrodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
Transient oligomeric species formed during the aggregation process of the 42-residue form of the amyloid-β peptide (Aβ42) are key pathogenic agents in Alzheimer’s disease (AD). To investigate the relationship bet...
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Article
Open AccessMethods of probing the interactions between small molecules and disordered proteins
It is generally recognized that a large fraction of the human proteome is made up of proteins that remain disordered in their native states. Despite the fact that such proteins play key biological roles and ar...
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Article
Simultaneous quantification of protein order and disorder
Nuclear magnetic resonance spectroscopy is transforming our views of proteins by revealing how their structures and dynamics are closely intertwined to underlie their functions and interactions. Compelling rep...
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Protocol
Quartz Microbalance Technology for Probing Biomolecular Interactions
Quartz crystal microbalance with dissipation monitoring (QCM-D) is a useful technique for observing the adsorption of molecules onto a protein-functionalized surface in real time. This technique is based on re...
