[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 …

Neuroprotective activity of selenium nanoparticles against the effect of amino acid enantiomers in Alzheimer's disease

D Vicente-Zurdo, S Rodríguez-Blázquez… - Analytical and …, 2022 - Springer
Abstract Alzheimer's disease (AD), the most prevalent neurodegenerative disease, is
characterized by extracellular accumulation of amyloid-beta protein (Aβ), which is believed …

Metal-ion-induced evolution of phenylalanine self-assembly: Structural polymorphism of novel metastable intermediates

D Bagchi, A Maity, SK De… - The Journal of Physical …, 2022 - ACS Publications
The self-assembly of aromatic amino acids has been widely studied due to their ability to
form well-defined amyloid-like fibrillar structures. Herein, for the first time, we report the …

Aromatic interactions directing peptide nano-assembly

S Sasidharan, V Ramakrishnan - Advances in Protein Chemistry and …, 2022 - Elsevier
Self-assembly is a process of spontaneous organization of molecules as a result of non-
covalent interactions. Organized self-assembly at the nano level is emerging as a powerful …

Differential effects of aromatic residues on amyloid formation and cytotoxicity of human IAPP

L Manathunga, A Zhyvoloup, A Baghai… - Biochemistry, 2022 - ACS Publications
Islet amyloid polypeptide (IAPP) is a 37-residue polypeptide hormone secreted by the
pancreatic β-cells. IAPP plays a role in glycemic regulation, but in the pre-type-2 diabetic …

[HTML][HTML] Contribution of the 12–17 hydrophobic region of islet amyloid polypeptide in self-assembly and cytotoxicity

M Fortier, M Côté-Cyr, V Nguyen, M Babych… - Frontiers in Molecular …, 2022 - frontiersin.org
The islet amyloid polypeptide (IAPP) is a 37-residue aggregation-prone peptide hormone
whose deposition as insoluble fibrils in the islets of Langerhans is associated with type II …

Effects of Charged Polyelectrolytes on Amyloid Fibril Formation of a Tau Fragment

M Islam, E Argueta, EP Wojcikiewicz… - ACS chemical …, 2022 - ACS Publications
The microtubule-associated protein tau is involved in more than 20 different neurological
disorders characterized by aberrant intracellular aggregation of tau in the brain. Here, we …

[HTML][HTML] Essential Role of Histidine for Rapid Copper (II)-Mediated Disassembly of Neurokinin B Amyloid

BM Jayawardena, L Peacey, R Gamsjaeger, CE Jones - Biomolecules, 2022 - mdpi.com
Neurokinin B is a tachykinin peptide involved in a diverse range of neuronal functions. It
rapidly forms an amyloid, which is considered physiologically important for efficient packing …

Isotope-edited vibrational circular dichroism study reveals a flexible N-terminal structure of islet amyloid peptide (NFGAIL) in amyloid fibril form: A site-specific local …

AC Unnikrishnan, G Shanmugam - Journal of Structural Biology, 2022 - Elsevier
The short peptide fragment NFGAIL (IAPf) is a well-known amyloidogenic peptide (22–27),
derived from human islet amyloid polypeptide (hIAPP), whose fibrillar structure is often used …

Challenges in experimental methods

ME Gąsior-Głogowska, N Szulc, M Szefczyk - Computer Simulations of …, 2022 - Springer
Experimental studies of amyloids encounter many challenges. There are many methods
available for studying proteins, which can be applied to amyloids: from basic staining …