Site-selective modification of peptide backbones
نویسندگان
چکیده
Exciting developments in the site-selective modification of peptide backbones are allowing an outstanding fine-tuning conformation, folding ability, and physico-chemical biological properties.
منابع مشابه
Site‐Selective Modification of Proteins with Oxetanes
Oxetanes are four-membered ring oxygen heterocycles that are advantageously used in medicinal chemistry as modulators of physicochemical properties of small molecules. Herein, we present a simple method for the incorporation of oxetanes into proteins through chemoselective alkylation of cysteine. We demonstrate a broad substrate scope by reacting proteins used as apoptotic markers and in drug f...
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For a reaction to be generally useful for protein modification, it must be site-selective and efficient under conditions compatible with proteins: aqueous media, low to ambient temperature, and at or near neutral pH. To engineer a reaction that satisfies these conditions is not a simple task. Olefin metathesis is one of most useful reactions for carbon-carbon bond formation, but does it fit the...
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M icrobes employ several catalytic strategies to transform conformationally f lexible peptide chains into rigidified scaffolds that possess antibiotic or toxin activity. Prominent examples include the biosynthesis of the -lactam antibiotics of the penicillin and cephalosporin families (1) and the maturation of vancomycin (2) where distinct structural modifications to the nascent peptide chains ...
متن کاملSite-selective chemical cleavage of peptide bonds.
Site-selective cleavage of extremely unreactive peptide bonds is a very important chemical modification that provides invaluable information regarding protein sequence, and it acts as a modulator of protein structure and function for therapeutic applications. For controlled and selective cleavage, a daunting task, chemical reagents must selectively recognize or bind to one or more amino acid re...
متن کاملA "tag-and-modify" approach to site-selective protein modification.
Covalent modification can expand a protein's functional capacity. Fluorescent or radioactive labeling, for instance, allows imaging of a protein in real time. Labeling with an affinity probe enables isolation of target proteins and other interacting molecules. At the other end of this functional spectrum, protein structures can be naturally altered by enzymatic action. Protein-protein interacti...
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ژورنال
عنوان ژورنال: Organic chemistry frontiers
سال: 2021
ISSN: ['2052-4110', '2052-4129']
DOI: https://doi.org/10.1039/d1qo00892g