A new class of pharmaceutical molecules--synthetic vaccines, synthetic diagnostics and peptide drugs--are emerging based on recent advances of peptide libraries, supramolecular chemistry and rational design. The molecules of this growing class have exciting potential, not met by classical drugs based on small molecules or recombinant proteins.
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Unlocking the Antibacterial Potential of Naphthalimide-Coumarins to Overcome Drug Resistance with Antibiofilm and Membrane Disruption Ability against .
ACS Appl Mater Interfaces
January 2025
Department of Chemistry and Biochemistry, Thapar Institute of Engineering and Technology, Patiala 147004, Punjab, India.
Resistance by bacteria to available antibiotics is a threat to human health, which demands the development of new antibacterial agents. Considering the prevailing conditions, we have developed a library of new naphthalimide-coumarin moieties as broad-spectrum antibacterial agents to fight against awful drug resistance. Preliminary studies indicate that compounds and display excellent antibacterial activity against , exceeding the performance of marketed drug amoxicillin.
View Article and Find Full Text PDFA coopetition-driven strategy of parallel/perpendicular aromatic stacking enabling metastable supramolecular polymerization.
Nat Commun
December 2024
School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi'an, 710072, China.
Metastable supramolecular polymerization under kinetic control has recently been recognized as a closer way to biosystem than thermodynamic process. While impressive works on metastable supramolecular systems have been reported, the library of available non-covalent driving modes is still small and a simple yet versatile solution is highly desirable to design for easily regulating the energy landscapes of metastable aggregation. Herein, we propose a coopetition-driven metastability strategy for parallel/perpendicular aromatic stacking to construct metastable supramolecular polymers derived from a class of simple monomers consisting of lateral indoles and aromatic core.
View Article and Find Full Text PDFMachine-Learning-Aided Engineering Hemoglobin as Carbene Transferase for Catalyzing Enantioselective Olefin Cyclopropanation.
JACS Au
December 2024
Key Laboratory of Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130023, P. R. China.
In this study, we developed a machine-learning-aided protein design strategy for engineering hemoglobin (VHb) as carbene transferase. A Natural Language Processing (NLP) model was used for the first time to construct an algorithm (EESP, enzyme enantioselectivity score predictor) and predict the enantioselectivity of VHb. We identified critical amino acid residue sites by molecular docking and established a simplified mutation library by site-saturated mutagenesis.
View Article and Find Full Text PDFInclusion of Cationic Amphiphilic Peptides in Fmoc-FF Generates Multicomponent Functional Hydrogels.
ACS Appl Bio Mater
December 2024
Department of Pharmacy and Interuniversity Research Centre on Bioactive Peptides "Carlo Pedone" (CIRPeB), University of Naples "Federico II", Via T. De Amicis 95, Naples 80145, Italy.
Article Synopsis
- Peptide building blocks can create supramolecular nanostructures that effectively deliver various drugs while their design impacts the ability of these structures to interact with specific drugs.
- The study focuses on hybrid cationic peptide hydrogels, combining a low-molecular-weight hydrogelator with different cationic amphiphilic peptides to analyze their structural properties.
- Findings indicate that the hydrogel's structure is primarily determined by the hydrogelator, while the peptides' alkyl chain lengths significantly influence the material's morphology, stiffness, and drug encapsulation capabilities.
RAS proteins are the most frequently mutated in cancer, yet they have proved extremely difficult to target in drug discovery, largely because interfering with the interaction of RAS with its downstream effectors comes up against the challenge of protein-protein interactions (PPIs). Sequence-defined synthetic oligomers could combine the precision and customisability of synthetic molecules with the size required to address entire PPI surfaces. We have adapted the phosphoramidite chemistry of oligonucleotide synthesis to produce a library of nearly one million non-nucleosidic oligophosphoester sequences (phosphoestamers) composed of units taken from synthetic supramolecular chemistry, and used a fluorescent-activated bead sorting (FABS) process to select those that inhibit the interaction between KRAS (the most prevalent, and undrugged, RAS mutant) and RAF, a downstream effector of RAS that drives cell proliferation.
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