The amyloid beta peptide: a chemist's perspective. Role in Alzheimer's and fibrillization

IW Hamley - Chemical reviews, 2012 - ACS Publications
This review is concerned with the role of fibrillization of the amyloid β (Aβ)-peptide in
Alzheimer's disease (AD). The perspective is that of a physical chemist, and one aim is to …

Computational methods and tools in antimicrobial peptide research

PGA Aronica, LM Reid, N Desai, J Li… - Journal of Chemical …, 2021 - ACS Publications
The evolution of antibiotic-resistant bacteria is an ongoing and troubling development that
has increased the number of diseases and infections that risk going untreated. There is an …

[HTML][HTML] Folding versus aggregation: polypeptide conformations on competing pathways

TR Jahn, SE Radford - Archives of biochemistry and biophysics, 2008 - Elsevier
Protein aggregation has now become recognised as an important and generic aspect of
protein energy landscapes. Since the discovery that numerous human diseases are caused …

Computer-aided antibody design

D Kuroda, H Shirai, MP Jacobson… - … engineering, design & …, 2012 - academic.oup.com
Recent clinical trials using antibodies with low toxicity and high efficiency have raised
expectations for the development of next-generation protein therapeutics. However, the …

Structural characterization of a soluble amyloid β-peptide oligomer

L Yu, R Edalji, JE Harlan, TF Holzman, AP Lopez… - Biochemistry, 2009 - ACS Publications
Alzheimer's disease (AD) is a neurodegenerative disorder that is linked to the presence of
amyloid β-peptides that can form insoluble fibrils or soluble oligomeric assemblies. Soluble …

Polymorphism in Alzheimer Aβ amyloid organization reflects conformational selection in a rugged energy landscape

Y Miller, B Ma, R Nussinov - Chemical reviews, 2010 - ACS Publications
Amyloids can have normal biological functions. 1r3 However, amyloidogenic proteins can
also form unwanted oligomeric or polymeric aggregates when disturbed from their native …

Nanostructure and molecular mechanics of spider dragline silk protein assemblies

S Keten, MJ Buehler - Journal of the Royal Society …, 2010 - royalsocietypublishing.org
Spider silk is a self-assembling biopolymer that outperforms most known materials in terms
of its mechanical performance, despite its underlying weak chemical bonding based on H …

Effects of All-Atom Molecular Mechanics Force Fields on Amyloid Peptide Assembly: The Case of Aβ16–22 Dimer

VH Man, X He, P Derreumaux, B Ji… - Journal of chemical …, 2019 - ACS Publications
We investigated the effects of 17 widely used atomistic molecular mechanics force fields
(MMFFs) on the structures and kinetics of amyloid peptide assembly. To this end, we …

Amyloid β-protein monomer folding: free-energy surfaces reveal alloform-specific differences

M Yang, DB Teplow - Journal of molecular biology, 2008 - Elsevier
Alloform-specific differences in structural dynamics between amyloid β-protein (Aβ) 40 and
Aβ42 appear to underlie the pathogenesis of Alzheimer's disease. To elucidate these …

Self-assembly of phenylalanine oligopeptides: insights from experiments and simulations

P Tamamis, L Adler-Abramovich, M Reches… - Biophysical journal, 2009 - cell.com
Studies of peptide-based nanostructures provide general insights into biomolecular self-
assembly and can lead material engineering toward technological applications. The …