Aglycon core

Mithramydn A binds to GC-rich or CG-rich DNA sequences and blocks DNMT methylation activity. Docking of mithramycin A into the DNMTl catalytic domain indicates that the trisaccharide of the inhibitor can fit into the putative cytosine pocket and the aglycon core is bound betv een the two arms that fasten the hemimethylated DNA. 

Unfortunately, the D-Ala-D-Ala binding region of the aglycon core is hardly accessible to chemical modification reactions. As a consequence, the options for the introduction of synthetic variations in the peptide core region are limited. We herein currently present established modifications of amino acids of the heptapeptide aglycon by chemical and biotechnological approaches. 

Tylosin 33 from Streptomyces fradiae is a representative member of the large family of 16-membered macrolide antibiotics commonly utilised in veterinary medicine. The aglycone core, tylactone 34 is constructed from two acetate, five propionate and one butyrate units [68, 69]. The processive mechanism for its biosynthesis was demonstrated by the pioneering contributions of Hutchinson... 

XI. Completion of Aglycon Core A Formal Synthesis of Polycavemoside A 204... 

In retrospect, our design for a seco acid precursor to the aglycon core... 

Daunorubicin Antitumor CYP129A2 (doxA)and CYP131A2(dnrQ) Streptomyces sp. strain C5 CIO, C13, C14 anthracycline glycone DNR precursor hydroxylations and likely aglycone core oxidation [794-796]... 

PCP-bound substrate specificity and are perhaps the most likely candidates for engineering modified variants of the aglycone core that may facilitate the production of novel glycopeptide antibiotics [317, 320,330, 331],... 

Figures 2 and 3 show that macrocyclic glycopeptides are simple enough so that their molecules can be easily modeled by small computers. They also show the variety of possible selector-selectand interactions including all possible chemical interactions from the strongest charge-charge (coulombic) interaction to the delicate shape recognition interaction within the cavities of the polypeptide aglycon core of the selectors.

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