17730-18-6

Usage

Uses

Used in Organic Synthesis:
Z-PRO-MET-OH is used as a reagent in organic synthesis for its ability to facilitate various chemical reactions, contributing to the formation of complex organic molecules.
Used in Pharmaceutical Research:
Z-PRO-MET-OH is used as a building block in the preparation of peptide and peptidomimetic compounds, which are essential in the development of new drugs and therapeutic agents.
Used in Peptide Synthesis:
Z-PRO-MET-OH is used as a protecting group for amino acids in peptide synthesis, ensuring the correct sequence and structure of the peptide during the synthesis process.
Used in Anti-Inflammatory Applications:
Z-PRO-MET-OH is studied for its potential as an anti-inflammatory agent, which could be beneficial in treating various inflammatory conditions.
Used in Anti-Cancer Applications:
Z-PRO-MET-OH is also being researched for its potential as an anti-cancer agent, indicating its possible role in the development of cancer treatments.

InChI:InChI=1/C18H24N2O5S/c1-26-11-9-14(17(22)23)19-16(21)15-8-5-10-20(15)18(24)25-12-13-6-3-2-4-7-13/h2-4,6-7,14-15H,5,8-12H2,1H3,(H,19,21)(H,22,23)

Upstream product

• 886981-23-3 benzyl (2S)-2-(1H-1,2,3-benzotriazol-1-ylcarbonyl)tetrahydro-1H-pyrrole-1-carboxylate 
• 63-68-3 L-methionine 
• 17445-57-7 Z-Pro-Met-OMe 
• 1148-11-4 N-Benzyloxycarbonyl-L-proline 

Downstream Products

• 110529-59-4 N-(benzyloxycarbonyl)-L-prolyl-L-methionine succinimido ester 
• 110512-43-1 methyl N--8-amino-2,6-anhydro-3,8-dideoxy-D-glycero-D-talo-octonate 

Relevant academic research and scientific papers

Novel Macrocyclic Peptidomimetics Targeting the Polo-Box Domain of Polo-Like Kinase 1

The polo-box domain (PBD) of Plk1 is a promising target for cancer therapeutics. We designed and synthesized novel phosphorylated macrocyclic peptidomimetics targeting PBD based on acyclic phosphopeptide PMQSpTPL. The inhibitory activities of 16e on Plk1-PBD is >30-fold higher than those of PMQSpTPL. Both 16a and 16e possess excellent selectivity for Plk1-PBD over Plk2/3-PBD. Analysis of the cocrystal structure of Plk1-PBD in complex with 16a reveals that the 3-(trifluoromethyl)benzoyl group in 16a interacts with Arg516 through a π-stacking interaction. This π-stacking interaction, which has not been reported previously, provides insight into the design of novel and potent Plk1-PBD inhibitors. Furthermore, 16h, a PEGlyated macrocyclic phosphopeptide derivative, induces Plk1 delocalization and mitotic failure in HeLa cells. Also, the number of phospho-H3-positive cells in a zebrafish embryo increases in proportion to the amount of 16a. Collectively, the novel macrocyclic peptidomimetics should serve as valuable templates for the design of potent and novel Plk1-PBD inhibitors.

Efficient peptide coupling involving sterically hindered amino acids

(Chemical Equation Presented) Hindered amino acids have been introduced into peptide chains by coupling N-(Cbz- and Fmoc-α-aminoacyl) benzotriazoles with amino acids, wherein at least one of the components was sterically hindered, to provide compounds 3a-e, (3c +3 c′), 5a-d, (5a + 5a′), 6a-c, (6b + 6b′), 8a-c, 9a-e, 10a-d, and (10a + 10a′) in isolated yields of 41-95% with complete retention of chirality as evidenced by NMR and HPLC analysis. The benzotriazole activation methodology is a new route for the synthesis of sterically hindered peptides. (Note: compound numbers written within brackets represent diastereomeric mixtures or racemates; compound numbers without brackets represent enantiomers.)