Progress in infrared spectroscopy as an efficient tool for predicting protein secondary structure

S Yang, Q Zhang, H Yang, H Shi, A Dong… - International Journal of …, 2022 - Elsevier
Infrared (IR) spectroscopy is a highly sensitive technique that provides complete information
on chemical compositions. The IR spectra of proteins or peptides give rise to nine …

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

G Wei, Z Su, NP Reynolds, P Arosio… - Chemical Society …, 2017 - pubs.rsc.org
Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

Congo Red and amyloids: history and relationship

EI Yakupova, LG Bobyleva, IM Vikhlyantsev… - Bioscience …, 2019 - portlandpress.com
Abstract Staining with Congo Red (CR) is a qualitative method used for the identification of
amyloids in vitro and in tissue sections. However, the drawbacks and artefacts obtained …

Multicomponent peptide assemblies

DM Raymond, BL Nilsson - Chemical Society Reviews, 2018 - pubs.rsc.org
Self-assembled peptide nanostructures have been increasingly exploited as functional
materials for applications in biomedicine and energy. The emergent properties of these …

On the lag phase in amyloid fibril formation

P Arosio, TPJ Knowles, S Linse - Physical Chemistry Chemical Physics, 2015 - pubs.rsc.org
The formation of nanoscale amyloid fibrils from normally soluble peptides and proteins is a
common form of self-assembly phenomenon that has fundamental connections with …

[HTML][HTML] Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation

FS Ruggeri, G Longo, S Faggiano, E Lipiec… - Nature …, 2015 - nature.com
Amyloids are insoluble protein fibrillar aggregates. The importance of characterizing their
aggregation has steadily increased because of their link to human diseases and material …

The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions

R Mezzenga, P Fischer - Reports on Progress in Physics, 2013 - iopscience.iop.org
The aggregation of proteins is of fundamental relevance in a number of daily phenomena,
as important and diverse as blood coagulation, medical diseases, or cooking an egg in the …

[HTML][HTML] Atomic force microscopy for single molecule characterisation of protein aggregation

FS Ruggeri, T Šneideris, M Vendruscolo… - Archives of biochemistry …, 2019 - Elsevier
The development of atomic force microscopy (AFM) has opened up a wide range of novel
opportunities in nanoscience and new modalities of observation in complex biological …

Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM

L Radamaker, S Karimi-Farsijani, G Andreotti… - Nature …, 2021 - nature.com
Systemic AL amyloidosis is a rare disease that is caused by the misfolding of
immunoglobulin light chains (LCs). Potential drivers of amyloid formation in this disease are …

Complete aggregation pathway of amyloid β (1-40) and (1-42) resolved on an atomically clean interface

PN Nirmalraj, J List, S Battacharya, G Howe, L Xu… - Science …, 2020 - science.org
To visualize amyloid β (Aβ) aggregates requires an uncontaminated and artifact-free
interface. This paper demonstrates the interface between graphene and pure water (verified …