Role of water in mediating the assembly of Alzheimer amyloid-β Aβ16− 22 protofilaments

MG Krone, L Hua, P Soto, R Zhou… - Journal of the …, 2008 - ACS Publications
The role of water in promoting the formation of protofilaments (the basic building blocks of
amyloid fibrils) is investigated using fully atomic molecular dynamics simulations. Our model …

Prediction of" hot spots" of aggregation in disease-linked polypeptides

NS De Groot, I Pallarés, FX Avilés, J Vendrell… - BMC Structural …, 2005 - Springer
Background The polypeptides involved in amyloidogenesis may be globular proteins with a
defined 3D-structure or natively unfolded proteins. The first class includes polypeptides such …

Designed aromatic homo-dipeptides: formation of ordered nanostructures and potential nanotechnological applications

M Reches, E Gazit - Physical biology, 2006 - iopscience.iop.org
Molecular self-assembly offers new routes for the fabrication of novel materials at the nano-
scale. Peptide-based nanostructures represent nano-objects of particular interest, as they …

Charge attraction and β propensity are necessary for amyloid fibril formation from tetrapeptides

L Tjernberg, W Hosia, N Bark, J Thyberg… - Journal of Biological …, 2002 - ASBMB
Amyloid fibrils in which specific proteins have polymerized into a cross-β-sheet structure are
found in about 20 diseases. In contrast to the close structural similarity of fibrils formed in …

Potential aggregation prone regions in biotherapeutics: a survey of commercial monoclonal antibodies

X Wang, TK Das, SK Singh, S Kumar - MAbs, 2009 - Taylor & Francis
Aggregation of a biotherapeutic is of significant concern and judicious process and
formulation development is required to minimize aggregate levels in the final product …

Molecular self-assembly of peptide nanostructures: mechanism of association and potential uses

M Reches, E Gazit - Current Nanoscience, 2006 - ingentaconnect.com
Molecular self-assembly offers unique directions for the fabrication of novel supramolecular
structures and advanced materials. The inspiration for the development of such structures is …

[HTML][HTML] IAPP in type II diabetes: Basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies

S Asthana, B Mallick, AT Alexandrescu, S Jha - Biochimica et Biophysica …, 2018 - Elsevier
Islet amyloid polypeptide (aka IAPP, amylin) is a 37 amino acid hormone that has long been
associated with the progression of type II diabetes mellitus (TIIDM) disease. The endocrine …

Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Aβ42 peptide

W Kim, MH Hecht - Proceedings of the National Academy of …, 2006 - National Acad Sciences
One hundred years ago, Alois Alzheimer observed a relationship between cognitive
impairment and the presence of plaque in the brains of patients suffering from the disease …

Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols

P Cao, DP Raleigh - Biochemistry, 2012 - ACS Publications
Islet amyloid polypeptide (IAPP, amylin) is responsible for amyloid formation in type 2
diabetes and in transplanted islets. The flavanol (−)-epigallocatechin-3-gallate [EGCG;(2 R …

Complete phenotypic recovery of an Alzheimer's disease model by a quinone-tryptophan hybrid aggregation inhibitor

R Scherzer-Attali, R Pellarin, M Convertino… - PLoS one, 2010 - journals.plos.org
The rational design of amyloid oligomer inhibitors is yet an unmet drug development need.
Previous studies have identified the role of tryptophan in amyloid recognition, association …