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Bismuth Bicycles
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DOI：10.1002/psc.70071.png)
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Abstract
En 中文
Bicyclic peptides are emerging as next generation therapeutics by combining the affinity and specificity of antibodies with the synthetic convenience of small molecules. Phage-encoded libraries of bicyclic peptides enable the discovery of high-affinity molecules against virtually any protein target. The generation of bicyclic peptides that advanced into clinical development involves the reaction of three cysteines in a peptide to a C-3-symmetric alkylating agent. In phage display, this chemical modification transforms a pool of conformationally flexible peptides into a library of structurally unique protein mimetics that are able to bind traditionally challenging protein surfaces like those with limited structural definition. In recent years, a new class of bicyclic peptides has emerged using a single atom-bismuth-in place of C-3-symmetric organic scaffolds, thus expanding into an unexplored chemical space at the intersection of inorganic chemistry and biology. This mini-review aims to reflect on the discovery, evolution and potential future applications of bismuth bicycle molecules.
Keywords:
CELL-PENETRATING PEPTIDES
HELICOBACTER-PYLORI
CYCLIC-PEPTIDES
BASES HSAB
SOFT ACIDS
ICP-MS
BINDING
CHEMISTRY
CYSTEINE
CONFORMATIONS
Journal
J
IF:
1.8
Papers:
32
Citations:
2.3K