Factors affecting the physical stability (aggregation) of peptide therapeutics
KL Zapadka, FJ Becher… - Interface …, 2017 - royalsocietypublishing.org
The number of biological therapeutic agents in the clinic and development pipeline has
increased dramatically over the last decade and the number will undoubtedly continue to …
increased dramatically over the last decade and the number will undoubtedly continue to …
Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)
It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …
Modulating α-Synuclein Liquid–Liquid Phase Separation: Published as part of the Biochemistry virtual special issue “Protein Condensates”
Liquid–liquid phase separation (LLPS) is a crucial phenomenon for the formation of
functional membraneless organelles. However, LLPS is also responsible for protein …
functional membraneless organelles. However, LLPS is also responsible for protein …
Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology
Abnormal aggregation of proteins into filamentous aggregates commonly associates with
many diseases, such as Alzheimer's disease, Parkinson's disease and type-2 diabetes …
many diseases, such as Alzheimer's disease, Parkinson's disease and type-2 diabetes …
Acceleration of α-synuclein aggregation by exosomes
Exosomes are small vesicles released from cells into extracellular space. We have isolated
exosomes from neuroblastoma cells and investigated their influence on the aggregation of α …
exosomes from neuroblastoma cells and investigated their influence on the aggregation of α …
Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification
Parkinson's disease (PD) is characterized by proteinaceous aggregates named Lewy
Bodies and Lewy Neurites containing α-synuclein fibrils. The underlying aggregation …
Bodies and Lewy Neurites containing α-synuclein fibrils. The underlying aggregation …
Stability matters, too–the thermodynamics of amyloid fibril formation
AK Buell - Chemical Science, 2022 - pubs.rsc.org
Amyloid fibrils are supramolecular homopolymers of proteins that play important roles in
biological functions and disease. These objects have received an exponential increase in …
biological functions and disease. These objects have received an exponential increase in …
The presence of an air–water interface affects formation and elongation of α-synuclein fibrils
The aggregation of human α-Synuclein (α-Syn) into amyloid fibrils is related to the onset of
multiple diseases termed synucleinopathies. Substantial evidence suggests that …
multiple diseases termed synucleinopathies. Substantial evidence suggests that …
[HTML][HTML] The role of surfaces on amyloid formation
F Grigolato, P Arosio - Biophysical Chemistry, 2021 - Elsevier
Interfaces can strongly accelerate or inhibit protein aggregation, destabilizing proteins that
are stable in solution or, conversely, stabilizing proteins that are aggregation-prone …
are stable in solution or, conversely, stabilizing proteins that are aggregation-prone …
The growth of amyloid fibrils: rates and mechanisms
AK Buell - Biochemical Journal, 2019 - portlandpress.com
Amyloid fibrils are β-sheet-rich linear protein polymers that can be formed by a large variety
of different proteins. These assemblies have received much interest in recent decades, due …
of different proteins. These assemblies have received much interest in recent decades, due …