[HTML][HTML] Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity

P Cao, P Marek, H Noor, V Patsalo, LH Tu, H Wang… - FEBS letters, 2013 - Elsevier
Pancreatic islet amyloid is a characteristic feature of type 2 diabetes. The major protein
component of islet amyloid is the polypeptide hormone known as islet amyloid polypeptide …

[HTML][HTML] Amyloids: from molecular structure to mechanical properties

M Schleeger, T Deckert-Gaudig, V Deckert, KP Velikov… - Polymer, 2013 - Elsevier
Many proteins of diverse sequence, structure and function self-assemble into
morphologically similar fibrillar aggregates known as amyloids. Amyloids are remarkable …

Tanshinones inhibit amyloid aggregation by amyloid-β peptide, disaggregate amyloid fibrils, and protect cultured cells

Q Wang, X Yu, K Patal, R Hu, S Chuang… - ACS chemical …, 2013 - ACS Publications
The misfolding and aggregation of amyloid-β (Aβ) peptides into amyloid fibrils is regarded
as one of the causative events in the pathogenesis of Alzheimer's disease (AD) …

Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis

A Lakshmanan, DW Cheong… - Proceedings of the …, 2013 - National Acad Sciences
The self-assembly of abnormally folded proteins into amyloid fibrils is a hallmark of many
debilitating diseases, from Alzheimer's and Parkinson diseases to prion-related disorders …

Effect of solvent on the self-assembly of dialanine and diphenylalanine peptides

AN Rissanou, E Georgilis, E Kasotakis… - The Journal of …, 2013 - ACS Publications
Diphenylalanine (FF) is a very common peptide with many potential applications, both
biological and technological, due to a large number of different nanostructures which it …

Amylin uncovered: a review on the polypeptide responsible for type II diabetes

K Pillay, P Govender - BioMed research international, 2013 - Wiley Online Library
Amylin is primarily responsible for classifying type II diabetes as an amyloid (protein
misfolding) disease as it has great potential to aggregate into toxic nanoparticles, thereby …

Exploring the Influence of Carbon Nanoparticles on the Formation of β-Sheet-Rich Oligomers of IAPP22–28 Peptide by Molecular Dynamics Simulation

J Guo, J Li, Y Zhang, X Jin, H Liu, X Yao - PLoS One, 2013 - journals.plos.org
Recent advances in nanotechnologies have led to wide use of nanomaterials in biomedical
field. However, nanoparticles are found to interfere with protein misfolding and aggregation …

Evidence of π‐stacking interactions in the self‐assembly of hIAPP22‐29

AA Profit, V Felsen, J Chinwong… - Proteins: Structure …, 2013 - Wiley Online Library
The role aromatic amino acids play in the formation of amyloid is a subject of controversy. In
an effort to clarify the contribution of aromaticity to the self‐assembly of human islet amyloid …

Inhibition of human islet amyloid polypeptide or amylin aggregation by two manganese-salen derivatives

S Bahramikia, R Yazdanparast - European journal of pharmacology, 2013 - Elsevier
Aggregation of human islet amyloid polypeptide (IAPP) into pancreatic fibrillar deposits has
been postulated to be one of the main contributors to impaired insulin secretion and …

Lipid bilayers significantly modulate cross-fibrillation of two distinct amyloidogenic peptides

N Gal, A Morag, S Kolusheva, R Winter… - Journal of the …, 2013 - ACS Publications
Amyloid plaques comprising misfolded proteins are the hallmark of several incurable
diseases, including Alzheimer's disease, type-II diabetes, Jacob–Creutzfeld disease, and …