99701-60-7

Upstream product

• 70533-96-9 N-tert-butoxycarbonyl-(L)-leucinamide 
• 61-90-5 L-leucine 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 63096-02-6 N-tert-butoxycarbonyl-L-leucine methyl ester 
• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 24424-99-5 di-tert-butyl dicarbonate 

Downstream Products

• 1357008-03-7 C₃₆H₅₅N₅O₇S 
• 1357007-77-2 C₃₀H₄₃N₅O₄S 
• 1357008-06-0 C₃₈H₅₉N₅O₇S 
• 1357008-66-2 C₃₆H₅₅N₅O₇S 
• 1357008-67-3 C₃₁H₄₇N₅O₅S 
• 1357007-79-4 C₃₁H₄₅N₅O₄S 
• 1357008-37-7 C₄₉H₆₄N₆O₉S 
• 1357008-38-8 C₄₂H₅₂N₆O₇S 
• 1357007-80-7 C₄₂H₅₀N₆O₆S 

Relevant academic research and scientific papers

Solid-phase synthesis via N-terminal attachment to the 2-chlorotrityl resin

Connection of a secondary amine to the 2-chlorotrityl resin followed by iterative saponification/coupling sequences provided a basis for generating focused peptidomimetic mini-libraries.

Comprehensive Synthesis of Amino Acid-Derived Thiazole Peptidomimetic Analogues to Understand the Enigmatic Drug/Substrate-Binding Site of P-Glycoprotein

A novel set of 64 analogues based on our lead compound 1 was designed and synthesized with an initial objective of understanding the structural requirements of ligands binding to a highly perplexing substrate-binding site of P-glycoprotein (P-gp) and their effect on modulating the ATPase function of the efflux pump. Compound 1, a stimulator of P-gp ATPase activity, was transformed to ATPase inhibitory compounds 39, 53, and 109. The ATPase inhibition by these compounds was predominantly contributed by the presence of a cyclohexyl group in lieu of the 2-aminobenzophenone moiety of 1. The 4,4-difluorocyclohexyl analogues, 53 and 109, inhibited the photolabeling by [125I]-IAAP, with IC50 values of 0.1 and 0.76 μM, respectively. Selected compounds were shown to reverse paclitaxel resistance in HEK293 cells overexpressing P-gp and were selective toward P-gp over CYP3A4. Induced-fit docking highlighted a plausible binding pattern of inhibitory compounds in the putative-binding pocket of P-gp. The current study underscores the stringent requirement by P-gp to bind to chemically similar molecules.

Total Synthesis of the Post-translationally Modified Polyazole Peptide Antibiotic Goadsporin

The structurally unique polyazole antibiotic goadsporin contains six heteroaromatic oxazole and thiazole rings integrated into a linear array of amino acids that also contains two dehydroalanine residues. An efficient total synthesis of goadsporin is repo

NOVEL PYRIDINE DERIVATIVES

The invention relates to a compound of formula (I) wherein R1 to R4 are defined as in the description and in the claims. The compound of formula (I) can be used as a medicament.

PYRIDIN- 2 -AMIDES USEFUL AS CB2 AGONISTS

The invention relates to a compound of formula (I) wherein R1 to R4 are defined as in the description and in the claims. The compound of formula (I) can be used as a medicament.

Synthesis of sansalvamide A peptidomimetics: Triazole, oxazole, thiazole, and pseudoproline containing compounds

Peptidomimetic-based macrocycles typically have improved pharmacokinetic properties over those observed with peptide analogs. Described are the syntheses of 13 peptidomimetic derivatives that are based on active sansalvamide A structures, where these analogs incorporate heterocycles (triazoles, oxazoles, thiazoles, or pseudoprolines) along the macrocyclic backbone. The syntheses of these derivatives employ several approaches that can be applied to convert a macrocyclic peptide into its peptidomimetic counterpart. These approaches include peptide modifications to generate the alkyne and azide for click chemistry, a serine conversion into an oxazole, a Hantzsch reaction to generate the thiazole, and protected threonine to generate the pseudoproline derivatives. Furthermore, we show that two different peptidomimetic moieties, triazoles, and thiazoles, can be incorporated into the macrocyclic backbone without reducing cytotoxicity: triazole and thiazole.