Proteostasis of islet amyloid polypeptide: a molecular perspective of risk factors and protective strategies for type II diabetes

D Milardi, E Gazit, SE Radford, Y Xu… - Chemical …, 2021 - ACS Publications
The possible link between hIAPP accumulation and β-cell death in diabetic patients has
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …

[HTML][HTML] Amyloid growth and membrane damage: Current themes and emerging perspectives from theory and experiments on Aβ and hIAPP

MFM Sciacca, C Tempra, F Scollo, D Milardi… - … et Biophysica Acta (BBA …, 2018 - Elsevier
Alzheimer's Disease (AD) and Type 2 diabetes mellitus (T2DM) are two incurable diseases
both hallmarked by an abnormal deposition of the amyloidogenic peptides Aβ and Islet …

Stabilizing off-pathway oligomers by polyphenol nanoassemblies for IAPP aggregation inhibition

P Nedumpully-Govindan, A Kakinen, EH Pilkington… - Scientific reports, 2016 - nature.com
Experimental studies have shown that many naturally occurring polyphenols have inhibitory
effect on the aggregation of several proteins. Here, we use discrete molecular dynamics …

Role of aromatic amino acids in amyloid self-assembly

IM Stanković, S Niu, MB Hall, SD Zarić - International journal of biological …, 2020 - Elsevier
Amyloids are proteins of a cross-β structure found as deposits in several diseases and also
in normal tissues (nails, spider net, silk). Aromatic amino acids are frequently found in …

The role of cholesterol in driving IAPP-membrane interactions

MFM Sciacca, F Lolicato, G Di Mauro, D Milardi… - Biophysical journal, 2016 - cell.com
Our knowledge of the molecular events underlying type 2 diabetes mellitus—a protein
conformational disease characterized by the aggregation of islet amyloid polypeptide (IAPP) …

Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP

MFM Sciacca, D Milardi, GML Messina, G Marletta… - Biophysical …, 2013 - cell.com
Disruption of the integrity of the plasma membrane by amyloidogenic proteins is linked to the
pathogenesis of a number of common age-related diseases. Although accumulating …

Amyloidogenic intrinsically disordered proteins: new insights into their self-assembly and their interaction with membranes

F Scollo, C La Rosa - Life, 2020 - mdpi.com
Aβ, IAPP, α-synuclein, and prion proteins belong to the amyloidogenic intrinsically
disordered proteins' family; indeed, they lack well defined secondary and tertiary structures …

[HTML][HTML] Silybins inhibit human IAPP amyloid growth and toxicity through stereospecific interactions

S García-Viñuales, IM Ilie, AM Santoro… - … et Biophysica Acta (BBA …, 2022 - Elsevier
Type 2 Diabetes is a major public health threat, and its prevalence is increasing worldwide.
The abnormal accumulation of islet amyloid polypeptide (IAPP) in pancreatic β-cells is …

[HTML][HTML] Serum albumin impedes the amyloid aggregation and hemolysis of human islet amyloid polypeptide and alpha synuclein

A Kakinen, I Javed, A Faridi, TP Davis, PC Ke - Biochimica et Biophysica …, 2018 - Elsevier
Protein aggregation is a ubiquitous phenomenon underpinning the origins of a range of
human diseases. The amyloid aggregation of human islet amyloid polypeptide (IAPP) and …

Solvent induced amyloid polymorphism and the uncovering of the elusive class 3 amyloid topology

Z Dürvanger, F Bencs, DK Menyhárd… - Communications …, 2024 - nature.com
Abstract Aggregation-prone-motifs (APRs) of proteins are short segments, which–as isolated
peptides-form diverse amyloid-like crystals. We introduce two APRs-designed variants of the …