Supramolecular helical systems: helical assemblies of small molecules, foldamers, and polymers with chiral amplification and their functions

E Yashima, N Ousaka, D Taura, K Shimomura… - Chemical …, 2016 - ACS Publications
In this review, we describe the recent advances in supramolecular helical assemblies
formed from chiral and achiral small molecules, oligomers (foldamers), and helical and …

Implications of peptide assemblies in amyloid diseases

PC Ke, MA Sani, F Ding, A Kakinen, I Javed… - Chemical Society …, 2017 - pubs.rsc.org
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …

Protein misfolding, functional amyloid, and human disease

F Chiti, CM Dobson - Annu. Rev. Biochem., 2006 - annualreviews.org
Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

Helical polymers: synthesis, structures, and functions

E Yashima, K Maeda, H Iida, Y Furusho… - Chemical …, 2009 - ACS Publications
The helix is the central structural motif in biological macromolecules, such as DNA and
proteins, and is also the ubiquitous object in nature from microscopic to macroscopic points …

Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism

L Nielsen, R Khurana, A Coats, S Frokjaer… - Biochemistry, 2001 - ACS Publications
In the search for the molecular mechanism of insulin fibrillation, the kinetics of insulin fibril
formation were studied under different conditions using the fluorescent dye thioflavin T …

Mechanism of thioflavin T binding to amyloid fibrils

R Khurana, C Coleman, C Ionescu-Zanetti… - Journal of structural …, 2005 - Elsevier
Thioflavin T is a benzothiazole dye that exhibits enhanced fluorescence upon binding to
amyloid fibrils and is commonly used to diagnose amyloid fibrils, both ex vivo and in vitro. In …

Conformational constraints for amyloid fibrillation: the importance of being unfolded

VN Uversky, AL Fink - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2004 - Elsevier
Recent reports give strong support to the idea that amyloid fibril formation and the
subsequent development of protein deposition diseases originate from conformational …

The protofilament structure of insulin amyloid fibrils

JL Jiménez, EJ Nettleton, M Bouchard… - Proceedings of the …, 2002 - National Acad Sciences
Under solution conditions where the native state is destabilized, the largely helical
polypeptide hormone insulin readily aggregates to form amyloid fibrils with a characteristic …

Amyloid fibrillogenesis: themes and variations

JC Rochet, PT Lansbury Jr - Current opinion in structural biology, 2000 - Elsevier
Recent progress has improved our knowledge of how proteins form amyloid fibrils. Both
'natively unfolded'and globular proteins have been shown to initiate fibrillization by adopting …

Characterization of the nanoscale properties of individual amyloid fibrils

JF Smith, TPJ Knowles, CM Dobson… - Proceedings of the …, 2006 - National Acad Sciences
We report the detailed mechanical characterization of individual amyloid fibrils by atomic
force microscopy and spectroscopy. These self-assembling materials, formed here from the …