Leucylalanine (Leu-Ala) is useful to produce non-electrolytic triorganotin (IV) derivatives (R3Sn(HL)) to study the models of metal-protein interactions.
Applicazioni
Leu-Ala hydrate has been used as a substrate in Tris-hydrochloride (HCl) buffer to analyze the leucine-alanine peptidase (LAP) activity in larvae.
Leucylalanine (Leu-Ala) is use to make non-electrolytic triorganotin(IV) derivatives (general formulae R3Sn(HL)) to study models of metal-protein interactions.
New triorganotin (IV) derivatives of dipeptides as models for metal-protein interactions: synthesis, structural characterization and biological studies.
Nath M, Pokharia S, Eng G, Song X, Kumar A.
Spectrochimica Acta Part A: Molecular Spectroscopy, 63, 66-75 (2006)
Proceedings of the National Academy of Sciences of the United States of America, 116(12), 5613-5622 (2019-03-08)
Many microbes acquire metabolites in a "feeding" process where complex polymers are broken down in the environment to their subunits. The subsequent uptake of soluble metabolites by a cell, sometimes called osmotrophy, is facilitated by transporter proteins. As such, the
Journal of medicinal chemistry, 50(10), 2399-2407 (2007-04-17)
Structure-based design and synthesis of a number of potent and selective memapsin 2 inhibitors are described. These inhibitors were designed based upon the X-ray structure of memapsin 2-bound inhibitor 3 that incorporates methylsulfonyl alanine as the P2-ligand and a substituted
Structure-based design, synthesis, and biological evaluation of a series of peptidomimetic beta-secretase inhibitors incorporating hydroxyethylamine isosteres are described. We have identified inhibitor 24 which has shown exceedingly potent activity in memapsin 2 enzyme inhibitory (K(i) 1.8 nM) and cellular (IC(50)=1
Folia histochemica et cytobiologica, 40(2), 135-136 (2002-06-12)
We have used the dipeptide Leu-Ala in an attempt to prevent the formation of ubiquitin-protein conjugates in U937 cells by inhibition of cellular E3 enzymes (ubiquitin ligases). Proteasome inhibitors induce the formation of perinuclear aggregates of ubiquitinated proteins and proteasomes
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