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Bioconjugate chemistry is the study of linking one molecule to another by chemical or biological means. The resulting complexes will typically be formed from at least one biomolecule, though they can also be purely synthetic molecules with a biological application.
Induction of helical structures in peptides have been shown to increase their membrane permeability and facilitate cargo delivery applications. Our study has shown that substitution of an unnatural amino acid into a mitochondrial-targeting peptide induces a helical conformation that is maintained even after conjugation onto carbon nanotubes and confers increased membrane permeability. This led to an increase in DNA delivery efficiencies and gene expression into the mitochondria of intact plants when used as a DNA delivery system.
The fluorophore-modified glucan, TPE-6BG3 adopts an extended, random-coiled form in DMSO, which does not fluoresce. The morphology of the TPE-6BG3 chemosensor changes drastically to a dynamic globule in aqueous media. The dynamic, “induced-fit” globule selectively and sensitively recognizes the medicinally-useful tetrasaccharide, acarbose via glucan-saccharide coaggregation.
Constructing polymer-based mimics on the surface of cells has potential to manipulate cell behavior, but precise control of grafting sites is challenging. Here, the authors report a method for site selected radical polymerization on cell surfaces by metabolic labelling.
Ribosomes have now been shown to accept certain initiator tRNAs acylated with aromatic foldamer–dipeptides thereby enabling the translation of a peptide or protein with a short aromatic foldamer at the N-terminus. Some foldamer–peptide hybrids could be cyclized to generate macrocycles that present conformationally restricted peptide loops.
Protein drugs are important therapies for many different diseases, but very few can be administered orally. Now, a cationic dendronized polymer has been shown to stabilize a therapeutic protein for delivery to the gut.
A new type of protein–polymer conjugate provides improved stability without detrimentally affecting bioactivity, and thus offers great potential for the development of new peptide-based drugs.