G. Meisl

Microfluidic antibody profiling after repeated SARS-CoV-2 vaccination links antibody affinity and concentration to impaired immunity and variant escape in patients on anti-CD-20 therapy

Molecular mechanism of α-synuclein aggregation on lipid membranes revealed.

This study reveals that lipids promote α-synuclein aggregation by enabling elongation, using a kinetic model to describe the co-aggregation process in vitro.

Self-replication of Abeta42 aggregates occurs on small and isolated fibril sites

The paper investigates A{beta}42 fibril self-replication using statistical mechanics and modeling, finding replication occurs on isolated small catalytic sites on the fibril surface.

α-Synuclein oligomers form by secondary nucleation

This study shows α-synuclein oligomers form via secondary nucleation on fibril surfaces, not from monomers, and this process is enhanced by agitation under physiological conditions.

Uncovering the universality of self-replication in protein aggregation and its link to disease.

The paper investigates self-replication in protein aggregates, finding it common in both functional and pathological contexts, with disease-related aggregates replicating faster than biological ones.

Understanding the role of memory re-activation and cross-reactivity in the defense against SARS-CoV-2

This study uses microfluidic antibody-affinity profiling to assess cross-reactive antibodies against SARS-CoV-2 in convalescent patients and pre-pandemic sera, finding low affinity and concentration against SARS-CoV-2 spike protein.

Mutations in two SARS-CoV-2 variants of concern reflect two distinct strategies of antibody escape

This study compares antibody escape mechanisms in SARS-CoV-2 alpha and beta variants, finding they use distinct strategies: alpha increases ACE2 binding affinity, while beta alters epitopes to reduce antibody access.

In vitro measurements of protein-protein interactions show that antibody affinity governs the inhibition of SARS-CoV-2 spike/ACE2 binding in convalescent serum

The paper measures how antibody affinity affects the inhibition of SARS-CoV-2 spike/ACE2 binding in convalescent serum using in vitro assays.

Perphenazine-macrocycle conjugates rapidly sequester the Aβ42 monomer and inhibit amyloid formation

This study designs perphenazine-cyclam conjugates that bind Aβ42 monomers, reducing toxic oligomers and fibrils, and inhibit amyloid formation even with pre-formed seeds.

Amplification, not spreading limits rate of tau aggregate accumulation in Alzheimer's disease

The paper quantifies tau aggregate replication rates in Alzheimer's disease and finds local replication, not spreading, limits tau accumulation in neocortical regions.

Microfluidic Antibody Affinity Profiling for In-Solution Characterisation of Alloantibody - HLA Interactions in Human Serum

This paper develops a microfluidic assay to directly measure antibody affinity and concentration in solution, applied to characterise alloantibody-HLA interactions in transplant patient sera.

Kinetic analysis reveals the rates and mechanisms of protein aggregation in a multicellular organism

This study quantitatively models protein aggregation in C. elegans using a molecular framework, showing that nucleation rates and stochasticity drive aggregation in vivo, consistent with in vitro findings.

Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses

The paper investigates the co-aggregation of S100A9 and Aβ42 amyloids using CDMS, microscopy, and kinetic analysis, revealing templating of S100A9 fibrils on Aβ42 surfaces.

Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide

This study investigates the dynamics of Aβ42 oligomers during amyloid fibril formation, revealing that most oligomers dissociate into monomers rather than forming fibrils.

Kinetic fingerprints differentiate anti-Aβ therapies

This study uses kinetic analysis and binding measurements to compare four anti-Aβ antibodies, showing aducanumab uniquely reduces Aβ oligomer flux.

Thermodynamic and kinetic design principles for protein aggregation inhibitors

This study develops a kinetic theory to identify thermodynamic and kinetic signatures of effective protein aggregation inhibitors.