Beilstein J. Org. Chem.2023,19, 434–439, doi:10.3762/bjoc.19.33
first reported example of the application of fluorinated aminophosphonates in cathepsinC inhibition studies. The new molecules show moderate inhibition of the cathepsinC enzyme, which opens the door to consider them as potential therapeutic agents. Overall, our findings provide a new avenue for the
development of fluorinated aminophosphonate-based inhibitors.
Keywords: aminophosphonates; cathepsinC; dipeptide; fluorine; solvolysis; Introduction
CathepsinC, also known as dipeptidyl peptidase I (DPPI) belongs to the family of lysosomal cysteine proteases encompassing 11 human enzymes (cathepsins B, C
, F, H, K, L, O, S, V, W, and X) [1]. CathepsinC is considered a good target for designing new anticancer agents with broad substrate specificity [2].
CathepsinC, which affects the processing of keratin, is of great importance in maintaining the structural organization of the epidermis, primarily
Beilstein J. Org. Chem.2018,14, 756–771, doi:10.3762/bjoc.14.64
][45][46]. On the contrary, cathepsinC functions as an aminodipeptidase and cathepsin H reveals next to its endopeptidase activity also aminomonopeptidase activity [44][46]. Due to the variety of the detected fragments, we suggest that the rat liver homogenate contained a similar mixture of homolog
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Graphical Abstract
Scheme 1:
Syntheses of GnRH-III–[(4Lys(Bu)/4Ser, 6Aaa, 8Lys(Dau=Aoa)] bioconjugates. a) (1) 2% hydrazine in D...