192378-05-5

Upstream product

• 63-91-2 L-phenylalanine 
• 123-11-5 4-methoxy-benzaldehyde 

Downstream Products

• 161563-31-1 N-(4-methoxybenzyl)-L-phenylalanine 
• 1322615-25-7 [1-(S)-benzyl-4-(4-(R)-benzyl-2-oxo-oxazolidin-3-yl)-2,4-dioxo-butyl]-(4-methoxy-benzyl)-carbamic acid benzyl ester 
• 439589-22-7 Cbz,PMB-Phe-OH 

Relevant academic research and scientific papers

The tandem chain extension aldol reaction used for synthesis of ketomethylene tripeptidomimetics targeting hPEPT1

The rationale for targeting the human di-/tripeptide transporter hPEPT1 for oral drug delivery has been well established by several drug and prodrug cases. The aim of this study was to synthesize novel ketomethylene modified tripeptidomimetics and to investigate their binding affinity for hPEPT1. Three related tripeptidomimetics of the structure H-Phe-ψ[COCH2]- Ser(Bz)-Xaa-OH were synthesized applying the tandem chain extension aldol reaction, where amino acid derived β-keto imides were stereoselectively converted to α-substituted γ-keto imides. In addition, three corresponding tripeptides, composed of amide bonds, were synthesized for comparison of binding affinities. The six investigated compounds were all defined as high affinity ligands (Ki-values 14C]Gly-Sar uptake in Caco-2 cells. Consequently, the ketomethylene replacement for the natural amide bond and α-side chain modifications appears to offer a promising strategy to modify tripeptidic structures while maintaining a high affinity for hPEPT1.

Synthesis of metallo-β-lactamase inhibitors

α-Amido trifluoromethyl alcohols and ketones were synthesised via two independent routes using the Ruppert Reagent (TMS-CF3) and shown to be inhibitors of metallo-β-lactamases.