Beilstein J. Org. Chem.2019,15, 577–583, doi:10.3762/bjoc.15.53
partial structures is driven by an interest in the chemistry of photoreactive amino acids and heterocycles that may find application in photoaffinitylabelling. Knowing the binding of a natural product to a biological target at atomic resolution, as it is the case for the cyclodepsipeptide jasplakinolide
A (1, Scheme 1) [1][2], is an ideal situation for the validation of the chemoselectivity and efficiency of photoaffinitylabelling. Recently, it has been determined by cryo-electron microscopy how jasplakinolide A (1) binds to F-actin and alters the actin skeleton in vivo, resulting in pronounced
-bromoabrine unit of 1 could be replaced by phototryptophan [7], whereas photo β-phenylalanine [8] could replace the β-tyrosine moiety. For photoaffinitylabelling studies with seragamides and geodiamolides, D-photophenylalanine could be incorporated.
In this paper we describe, as the first step of such an
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Graphical Abstract
Scheme 1:
Actin-binding cyclodepsipeptides, photo amino acids, retrosynthetic cuts of polyketide 7 leading to...
Beilstein J. Org. Chem.2018,14, 1890–1900, doi:10.3762/bjoc.14.163
accuracy. We are concluding from this study that photolabeling of FimH with sugar diazirines has only very limited success and cannot be regarded a facile approach for covalent modification of FimH.
Keywords: diazirines; docking; FimH; lectin ligands; mannosides; mass spectrometry; photoaffinitylabelling
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Graphical Abstract
Figure 1:
Principle of photoaffinity labeling of proteins with diazirine derivatives. Photolabile ligands are...