[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 …

Amyloid-like conformation and interaction for the self-assembly in barnacle underwater cement

M Nakano, K Kamino - Biochemistry, 2015 - ACS Publications
Barnacles are unique marine sessile crustaceans and permanently attach to various foreign
surfaces during most of their lifespan. The protein complex secreted from their body and …

Danshen (Salvia miltiorrhiza) water extract shows potential neuroprotective effects in Caenorhabditis elegans

CW Yuen, V Murugaiyah, N Najimudin… - Journal of …, 2021 - Elsevier
Ethnopharmacological relevance Danshen, is a traditional Chinese medicine obtained from
the dried root and rhizome of Salvia miltiorrhiza Bunge. It is known to be used for …

Short peptide amyloid organization: stabilities and conformations of the islet amyloid peptide NFGAIL

D Zanuy, B Ma, R Nussinov - Biophysical journal, 2003 - cell.com
Experimentally, short peptides have been shown to form amyloids similar to those of their
parent proteins. Consequently, they present useful systems for studies of amyloid …

Modulation of S6 fibrillation by unfolding rates and gatekeeper residues

JS Pedersen, G Christensen, DE Otzen - Journal of molecular biology, 2004 - Elsevier
We present a protein engineering analysis of the fibrillation of a protein from a thermophilic
organism, the 101 residue S6 from Thermus thermophilus. When agitated, S6 fibrillates at …

Sequence determinants of bacterial amyloid formation

X Wang, MR Chapman - Journal of molecular biology, 2008 - Elsevier
Amyloids are proteinaceous fibers commonly associated with neurodegenerative diseases
and prion-based encephalopathies. Many different polypeptides can form amyloid fibers …

Specificity in transmembrane helix-helix interactions mediated by aromatic residues

N Sal-Man, D Gerber, I Bloch, Y Shai - Journal of Biological Chemistry, 2007 - ASBMB
Aromatic residues have been previously shown to mediate the self-assembly of different
soluble proteins through π-π interactions (McGaughey, GB, Gagne, M., and Rappe, AK …

NFGAIL amyloid oligomers: the onset of beta-sheet formation and the mechanism for fibril formation

W Hoffmann, K Folmert, J Moschner… - Journal of the …, 2018 - ACS Publications
The hexapeptide NFGAIL is a highly amyloidogenic peptide, derived from the human islet
amyloid polypeptide (hIAPP). Recent investigations indicate that presumably soluble hIAPP …

Protein aggregation in Escherichia coli: role of proteases

R Rosen, D Biran, E Gur, D Becher… - FEMS microbiology …, 2002 - academic.oup.com
Protein aggregation is involved in several human diseases, and presumed to be an
important process in protein quality control. In bacteria, aggregation of proteins occurs …

Role of amino acid hydrophobicity, aromaticity, and molecular volume on IAPP (20–29) amyloid self‐assembly

TM Doran, AJ Kamens, NK Byrnes… - Proteins: Structure …, 2012 - Wiley Online Library
Aromatic amino acids strongly promote cross‐β amyloid formation; whether the
amyloidogenicity of aromatic residues is due to high hydrophobicity and β‐sheet propensity …