Crosslinked polymethacrylate absorbent with phenylalanine and stearate pendants

Herein, we report a new class of oil absorbents via conventional free radical polymerization method to prepare polymethacrylate gels with a range of crosslinking density having both phenylalanine and stearate moieties in the gel matrix. Analogue crosslinked gel was also synthesized with only stearate pendants without phenylalanine. Solvent absorbing capacity of gels was studied in various solvents with different dielectric constants. The mechanical property and morphology of the absorbents were studied by rheological method and field emission scanning electron microscopy, respectively. Modulation of porosity, absorption capacity and mechanical property of the absorbent were achieved with the variation of crosslinking density. The side chain pendants in the absorbent played an important role toward the solvent uptake capabilities. The absorbent readily can uptake 66 times chloroform and 14 times petrol of its dry weight at room temperature. Overall, the solvent uptake capacity of a new class of absorbents was well studied in this report.</p

Helical Superstructures from the Hierarchical Self-Assembly of Coil–Coil Block Copolymer Guided by Side Chain Amyloid-β(17–19) LVF Peptide

The rational design of precisely controlled hierarchical chiral nanostructures from synthetic polymers garnered inspiration from sophisticated biological materials. Since chiral peptide motifs induce helix formation in macromolecules, herein we report the synthesis of a novel type of hybrid polymer consisting of a β-sheet forming a LVF [L = leucine, V = valine, and F = phenylalanine] tripeptide pendant polymethacrylate block and a poly­[poly­(ethylene glycol) methyl ether methacrylate] (PPEGMA) block. The designed block copolymer self-organized into helical superstructures with a left-handed twisting sense, as visualized by field emission scanning electron microscopy, transmission electron microscopy, and atomic force microscopy. This intriguing hierarchical self-assembly is driven by the minimalistic peptide motif that itself has a high propensity to adopt an antiparallel β-sheet conformation. We also report the generation of a diverse array of nanostructures, including spherical micelles, spindle micelles, rod-like micelles, vesicles, helical supramolecular fibers, and helical toroids via self-assembly of the designed block copolymer in tetrahydrofuran/water mixed solvents. To realize the observable helical superstructure, a twisted two-dimensional core–shell tape is proposed as a structure model in which the peptide segments form an antiparallel β-sheet with a polymer shell. The findings contribute to the advancement of a helical polymer or the superhelical self-assembly of polymers, paving the way for diverse applications in materials science and related fields

Amyloid β‑Peptide Segment Conjugated Side-Chain Proline-Based Polymers as Potent Inhibitors in Lysozyme Amyloidosis

Developing effective amyloidosis inhibitors poses a significant challenge due to the dynamic nature of the protein structures, the complex interplay of interfaces in protein–protein interactions, and the irreversible nature of amyloid assembly. The interactions of amyloidogenic polypeptides with other peptides play a pivotal role in modulating amyloidosis and fibril formation. This study presents a novel approach for designing and synthesizing amyloid interaction surfaces using segments derived from the amyloid-promoting sequence of amyloid β-peptide [VF(Aβ(18–19)/FF(Aβ(19–20)/LVF(Aβ(17–19)/LVFF(Aβ(17–20)], where VF, FF, LVF and LVFF stands for valine phenylalanine dipeptide, phenylalanine phenylalanine dipeptide, leucine valine phenylalanine tripeptide and leucine valine phenylalanine phenylalanine tetrapeptide, respectively. These segments are conjugated with side-chain proline-based methacrylate polymers serving as potent lysozyme amyloidosis inhibitors and demonstrating reduced cytotoxicity of amyloid aggregations. Di-, tri-, and tetra-peptide conjugated chain transfer agents (CTAs) were synthesized and used for the reversible addition–fragmentation chain transfer polymerization of tert-butoxycarbonyl (Boc)-proline methacryloyloxyethyl ester (Boc-Pro-HEMA). Deprotection of Boc-groups from the side-chain proline pendants resulted in water-soluble polymers with defined peptide chain ends as peptide–polymer bioconjugates. Among them, the LVFF-conjugated polymer acted as a potent inhibitor with significantly suppressed lysozyme amyloidosis, a finding supported by comprehensive spectroscopic, microscopic, and computational analyses. These results unveil the synergistic effect between the segment-derived amyloid β-peptide and side-chain proline-based polymers, offering new prospects for targeting lysozyme amyloidosis