Poly(2,3-Dihydrofuran): A Strong, Biorenewable, and Degradable Thermoplastic Synthesized via Room Temperature Cationic Polymerization.

Creation of strong and tough plastics from sustainable and biorenewable resources is a significant challenge in polymer science. This challenge is further complicated when attempting to make these materials using an economically viable process, which is often hindered by the production and availability of chemical feedstocks and the efficiency of the monomer synthesis. Herein, we report the synthesis and characterization of a strong thermoplastic made from 2,3-dihydrofuran (DHF), a monomer made in one step from 1,4-butanediol, a bioalcohol already produced on the plant scale.

Exploring the influence of brilliant blue G on amyloid fibril formation of lysozyme.

Evidence suggests that amyloid fibril mitigation/inhibition is considered a promising approach toward treating amyloid diseases. In this work, we first examined how amyloid fibrillogenesis of lysozyme was affected by BBG, a safe triphenylmethane compound with nice blood-brain-barrier-permeability, and found that shorter fibrillar species were formed in the lysozyme samples treated with BBG. Next, alterations in the features including the secondary as well as tertiary structure, extent of aggregation, and molecular distribution of lysozyme triggered by the addition of BBG were examined by various spectroscopic techniques, right-angle light scattering, dynamic light scattering, and SDS-PAGE.

Dye-Affinity Nanofibrous Membrane for Adsorption of Lysozyme: Preparation and Performance Evaluation.

Polyacrylonitrile (PAN) nanofibrous membrane was prepared by an electrospinning technique. After heat treatment and alkaline hydrolysis, the weak ion exchange membrane was grafted with chitosan molecule and then covalently immobilized with a Cibacron Blue F3GA (CB). Fibre diameter, porosity and pore size of the membrane and immobilized dye density were characterized.

Examining the inhibitory potency of food additive fast green FCF against amyloid fibrillogenesis under acidic conditions.

More than thirty human proteins and/or peptides can fold incorrectly to form amyloid deposits associated with several protein aggregation diseases. No cure is currently available for treating these diseases. This work is aimed at examining the inhibitory potency of fast green FCF, a biocompatible dye, toward the fibrillogenesis/aggregation of lysozyme.