Linear monodisperse 18- and 20-mer acrylates are obtained via consecutive synthesis of two sequence-defined acrylate 9- and 10-mers, followed by disulfide coupling utilizing reversible addition-fragmentation chain transfer (RAFT) end group chemistry. The sequence-defined oligoacrylates are accessed via consecutive single (SUMI) and multiple (MUMI) unit monomer insertions through RAFT polymerization, using the extensive acrylate monomer library as functional building blocks. Aminolysis of the trithiocarbonate macroRAFT end group and in situ oxidation of the thiols to form a disulfide bridge lead to the formation of 18- and 20-mer acrylates. In this approach, one or multiple acrylate building blocks can be inserted in each step by chain extension to form a stable carbon-carbon backbone. Isolation of the targeted monodisperse oligomers, from the statistical mixtures obtained at first, is performed by flash column chromatography with high efficiency. It is shown that the SUMI and MUMI strategy, when combined with flash column chromatography separation, is highly efficient and allows to construct monodisperse materials of very considerable length starting from cheap and very versatile building blocks.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/acsmacrolett.7b00430 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Mixed-mode separation of antisense oligonucleotides using a single column with complementary anion-exchange and hydrophobic interaction chromatography approaches.
J Chromatogr A
December 2024
Genetics Guided Dementia Discovery (G2D2), Eisai, Inc. 35 Cambridge Park Drive, Suite 200, Cambridge, MA, 02140, USA.
The current study investigates the use of mixed-mode chromatography as a combination of anion-exchange (AEX) and hydrophobic interaction chromatography (HIC) for the analysis and purification of single-stranded antisense oligonucleotides with stereo-controlled phosphorothioate inter- nucleotide linkages. Initially a Scherzo-SS-C18 trimodal stationary phase with reversed-phase/AEX/ cation-exchange (CEX) functionalities is systematically evaluated to reveal the presence of U-shaped retention composed of two retention modes namely AEX and HIC, where the latter was also observed on related trimodal Scherzo SM and SW analogues. For the first time, retention and separation of deprotected oligonucleotides was described on a single mixed-mode column using a combination of AEX and HIC.
View Article and Find Full Text PDFHeterologous Prime-Boost with Immunologically Orthogonal Protein Nanoparticles for Peptide Immunofocusing.
ACS Nano
July 2024
School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
Protein nanoparticles are effective platforms for antigen presentation and targeting effector immune cells in vaccine development. Encapsulins are a class of protein-based microbial nanocompartments that self-assemble into icosahedral structures with external diameters ranging from 24 to 42 nm. Encapsulins from were designed to package bacterial RNA when produced in and were shown to have immunogenic and self-adjuvanting properties enhanced by this RNA.
View Article and Find Full Text PDFAPPI-Derived Cyclic Peptide Enhances Aβ42 Aggregation and Reduces Aβ42-Mediated Membrane Destabilization and Cytotoxicity.
ACS Chem Neurosci
September 2023
Avram and Stella Goldstein-Goren Department of Biotechnology Engineering and the National Institute of Biotechnology in the Negev, Ben-Gurion University of the Negev, P.O. Box 653, Beer-Sheva 84105, Israel.
An amyloid precursor protein inhibitor (APPI) and amyloid beta 42 (Aβ42) are both subdomains of the human transmembrane amyloid precursor protein (APP). In the brains of patients with Alzheimer's disease (AD), Aβ42 oligomerizes into aggregates of various sizes, with intermediate, low-molecular-weight Aβ42 oligomers currently being held to be the species responsible for the most neurotoxic effects associated with the disease. Strategies to ameliorate the toxicity of these intermediate Aβ42 oligomeric species include the use of short, Aβ42-interacting peptides that either inhibit the formation of the Aβ42 oligomeric species or promote their conversion to high-molecular-weight aggregates.
View Article and Find Full Text PDFCryoEM structure and Alphafold molecular modelling of a novel molluscan hemocyanin.
PLoS One
June 2023
School of Biosciences, Cardiff University, Cardiff, United Kingdom.
Article Synopsis
- - Hemocyanins are multi-protein complexes in the blood of arthropods and molluscs, functioning as oxygen transporters, with structures featuring decameric building blocks that can assemble in larger structures (didecamer, tridecamer) displaying specific symmetries.
- - The study utilized cryo-electron microscopy (cryoEM) to examine hemocyanin structures from the slipper limpet at high resolution, revealing unique assembly configurations and suggesting the presence of various higher-order multimers.
- - By using Alphafold for molecular modeling, researchers highlighted the structural similarities between the studied hemocyanin and other known hemocyanins, providing insight into the assembly mechanisms and functional units involved
Humanizing plant-derived snakins and their encrypted antimicrobial peptides.
Biochimie
August 2022
Department of Phytopharmaceuticals, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran; Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran. Electronic address:
Due to safety restrictions, plant-derived antimicrobial peptides (AMPs) need optimization to be consumed beyond preservatives. Herein, 175 GASA-domain-containing snakins were analyzed. Factors including charge, hydrophobicity, helicity, hydrophobic moment (μH), folding enthalpy, folding heat capacity, folding free energy, therapeutic index, allergenicity, and bitterness were considered.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!