178972-26-4

Upstream product

• 32315-10-9 bis(trichloromethyl) carbonate 
• 94838-55-8 tert-butyl (4-aminobenzyl)carbamate 
• 33233-67-9 4-(tert-Butoxycarbonylaminomethyl)benzoic acid 

Downstream Products

• 959924-63-1 (4-{3,5-bis-[4-(tert-butoxycarbonylamino-methyl)-phenyl]-2,4,6-trioxo-[1,3,5]triazinan-1-yl}-benzyl)carbamic acid tert-butyl ester 
• 1620568-11-7 C₂₂H₃₁N₃O₆ 
• 1620568-04-8 4-(2-carboxymethyl-4-oxoazetidine-1-carboxamido)phenylmethanaminium 2,2,2-trifluoroacetate 
• 1620568-12-8 C₂₅H₂₉N₃O₆ 
• 1620568-13-9 C₁₈H₂₃N₃O₆ 
• 1620568-14-0 C₂₇H₃₂N₄O₇ 
• 1620568-15-1 C₂₀H₂₆N₄O₇ 
• 1620568-06-0 4-(2-(2-(carboxymethylamino)-2-oxoethyl)-4-oxoazetidine-1-carboxamido)phenylmethanaminium 2,2,2-trifluoroacetate 
• 1620568-17-3 C₁₇H₂₁N₃O₆ 
• 1620568-08-2 (S)-(2-carboxy-4-oxoazetidine-1-carboxamido)phenylmethanaminium 2,2,2-trifluoroacetate 
• 1620568-16-2 C₂₄H₂₇N₃O₆ 

Relevant academic research and scientific papers

Targeting integrins αvβ3 and α5β1 with new β-lactam derivatives

The αvβ3 and α5β 1 integrins are widely expressed in different cancer types and recognize the tripeptide Arg-Gly-Asp (RGD) motif present in several extracellular matrix proteins. We report here the design, synthesis and biological activity of some new β-lactam derivatives specifically designed to target integrins. The new molecules contain the azetidinone as the only cyclic framework armed with carboxylic acid and amine terminals spaced from 9 to 14 atoms to switch on recognition by integrins. All tested molecules showed a concentration-dependent enhancement in fibronectin-mediated adhesion of K562 and SK-MEL-24 cells; in particular 1, expressed a higher affinity towards α5β1 integrin (EC50 of 12 nM) and 2 was more selective for integrin αvβ3 (EC 50 of 11 nM).

Small multivalent architectures mimicking homotrimers of the TNF superfamily member CD40L: Delineating the relationship between structure and effector function

Synthetic multivalent ligands, owing to the presence of multiple copies of a recognition motif attached to a central scaffold, can mediate clustering of cell surface receptors and thereby function as effector molecules. This paper dissects the relationship between structure and effector function of synthetic multivalent ligands targeting CD40, a cell surface receptor of the tumor necrosis factor receptor (TNF-R) superfamily. Triggering CD40 signaling in vivo can be used to enhance immunity against intracellular pathogens or tumors. A series of multimeric molecules has been prepared by systematically varying the shape and the valency of the central scaffold, the nature and the length of the linker as well as the sequence of the receptor binding motif. The data reported here (i) suggest that radial distribution of CD40-binding units and C 3-symmetry are preferred for optimal binding to CD40 and signaling, (ii) underscore the importance of choosing an appropriate linker to connect the receptor binding motif to the central scaffold, and (iii) show the versatility of planar cyclic α- and β-peptides as templates for the design of CD40L mimetics. In particular, the (Ahx)3-B trimeric scaffold-linker combination equally accommodated binding elements derived from distinct CD40L hot-spot regions including AA″ loop and β-strand E. The use of miniCD40Ls such as those reported here is complementary to other approaches (recombinant ligands, agonistic anti-receptor antibodies) and may find interesting therapeutic applications. Furthermore, the results disclosed in this paper provide the basis for future design of other TNF family member mimetics.