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• W2918790987 abstract "Synthetic pseudopeptides that fit well with the active site architecture allow the most effective binding to enzymes, similar to native substrates in high-energy transition states. Phosphinic acid peptide analogs that comprise the tetrahedral phosphorus moiety introduced to replace an internal amide bond exert such an isosteric or isoelectronic resemblance, combined with providing other advantageous features, for example, metal complexing properties. Accordingly, they are capable of inhibiting metal-dependent enzymes involved in biological functions in eukaryotic and prokaryotic cells. These enzymes are associated with notorious human diseases, such as cancer, e.g., matrix metalloproteinases, or are etiological factors of protozoal and bacterial infections, e.g., metalloaminopeptidases. The affinity and selectivity of these compounds can be conveniently adjusted, either by structural modification of dedicated side chains or by backbone elongation to enhance specific interactions with the corresponding binding pockets. Recent approaches to the synthesis of these compounds are illustrated by examples of the preparation of rationally designed structures of inhibitors of particular enzymes. Activity against appealing enzymatic targets is presented, along with the molecular mechanisms of action and therapeutic implications. Innovative aspects of phosphinic peptide application, e.g., as activity-based probes, and ligands of complexes of radioisotopes for nuclear medicine are also outlined." @default.
• W2918790987 created "2019-03-11" @default.
• W2918790987 creator A5027796694 @default.
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• W2918790987 date "2019-05-01" @default.
• W2918790987 modified "2023-09-30" @default.
• W2918790987 title "Recent developments in the synthesis and applications of phosphinic peptide analogs" @default.
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• W2918790987 doi "https://doi.org/10.1016/j.bmcl.2019.02.034" @default.
• W2918790987 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30846252" @default.
• W2918790987 hasPublicationYear "2019" @default.
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