A new era for understanding amyloid structures and disease

MG Iadanza, MP Jackson, EW Hewitt… - … reviews Molecular cell …, 2018 - nature.com
The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

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 …

A guide to studying protein aggregation

JAJ Housmans, G Wu, J Schymkowitz… - The FEBS …, 2023 - Wiley Online Library
Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

Evaluation of peptide/protein self-assembly and aggregation by spectroscopic methods

MF Pignataro, MG Herrera, VI Dodero - Molecules, 2020 - mdpi.com
The self-assembly of proteins is an essential process for a variety of cellular functions
including cell respiration, mobility and division. On the other hand, protein or peptide …

Amyloid β protein and Alzheimer's disease: When computer simulations complement experimental studies

J Nasica-Labouze, PH Nguyen, F Sterpone… - Chemical …, 2015 - ACS Publications
Alzheimer's disease (AD) challenges our society with an annual estimated cost of $1.08
trillion in the United States alone by 2050. 1 AD is a progressive irreversible neurological …

Use of Bombyx mori silk fibroin in tissue engineering: From cocoons to medical devices, challenges, and future perspectives

A Bucciarelli, A Motta - Biomaterials Advances, 2022 - Elsevier
Silk fibroin has become a prominent material in tissue engineering (TE) over the last 20
years with almost 10,000 published works spanning in all the TE applications, from skeleton …

[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 …

Effects of in vivo conditions on amyloid aggregation

MC Owen, D Gnutt, M Gao, SKTS Wärmländer… - Chemical Society …, 2019 - pubs.rsc.org
One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …

Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1–42 aggregates

K Zhaliazka, M Matveyenka, D Kurouski - The FEBS journal, 2023 - Wiley Online Library
Abrupt aggregation of amyloid β1‐42 (Aβ) peptide is a hallmark of Alzheimer's disease (AD),
a severe pathology that affects more than 44 million people worldwide. A growing body of …

Lipids uniquely alter rates of insulin aggregation and lower toxicity of amyloid aggregates

M Matveyenka, S Rizevsky, JP Pellois… - Biochimica et Biophysica …, 2023 - Elsevier
Amyloid formation is a hallmark of many medical diseases including diabetes type 2,
Alzheimer's and Parkinson diseases. Under these pathological conditions, misfolded …