123441-84-9

Upstream product

• 501-53-1 benzyl chloroformate 
• 1155-64-2 N₆-[(benzyloxy)carbonyl]-L-lysine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 56-87-1 L-lysine 
• 2389-45-9 Boc-Lys(Z)-OH 
• 100-46-9 benzylamine 

Downstream Products

• 246869-37-4 H2N-L-Lys(ε-Cbz)-CONHCH2Ph 
• 1456905-62-6 2-(N-tert-butoxycarbonylamino)-6-hydroxy-N-benzylhexanamide 
• 1446689-47-9 6-amino-2-(N-tert-butoxycarbonylamino)-N-benzylhexanamide 
• 1456906-91-4 2-(N-benzenecarbonylamino)-6-(trans-2-phenylcyclopropan-1-amino)-N-benzylhexanamide trifluoroacetate 
• 1456905-59-1 2-(N-benzenecarbonylamino)-6-(O-methanesulfonyl)-N-benzylhexanamide 
• 1456905-57-9 (S)-N-(1-(benzylamino)-6-hydroxy-1-oxohexan-2-yl)benzamide 
• 1456905-55-7 6-amino-2-(benzenecarbonyl)amino-N-(benzyl)hexanamide 
• 1456905-53-5 2-(N-benzenecarbonylamino)-6-(N-benzyloxycarbonylamino)-N-benzylhexanamide 

Relevant academic research and scientific papers

Alkylated histidine based short cationic antifungal peptides: Synthesis, biological evaluation and mechanistic investigations

Current clinically used antifungal agents suffer from several drawbacks that have urgently necessitated the development of new antifungal agents with unusual mechanisms of action. In this context, antifungal peptides (AFPs) open up new perspectives in drug design by providing an entire range of highly selective and nontoxic pharmaceuticals. Here, we report the development of novel short AFPs with the synthesis of two series of tripeptide based compounds named as His(2-alkyl)-Arg-Lys (series I) and His(2-alkyl)-Arg-Arg (series II). The series II peptides were found to be selectively active against Cryptococcus neoformans whereas some peptides displayed encouraging activities against other fungal strains such as Candida albicans, Candida kyfer, Aspergillus Niger and Neurospora crassa. The cytotoxic experiments were performed on active compounds using Hek-293 and HeLa cells which exhibited negligible cytotoxic effect up to the highest test concentration. Further, the most potent peptide was subjected to mechanistic studies using TEM analysis. Two sets of SUVs mimicking microbial membrane and mammalian membrane were treated with the most potent peptide. The results of this study were found to be perfectly in corroboration with the antifungal activity in relation to the differences between microbial and mammalian cell membrane composition, thereby, indicating that the reported peptides may also be less susceptible to the common mechanisms of drug resistance.

LSD1-SELECTIVE INHIBITOR HAVING LYSINE STRUCTURE

A primary object of the present invention is to provide a novel compound having LSD1-selective inhibitory activity and having an antitumor/anticancer action, an antiviral action, and the like. As means for achieving such object, provided is a compound represented by the following formula (I) or a pharmaceutically acceptable salt thereof: [in the formula, R1 to R5, A, and *1 to *3 are as defined in Description].

Exploring the Phe-Gly Dipeptide-derived Piperazinone Scaffold in the search for Antagonists of the Thrombin receptor PAR1

A series of Phe-Gly dipeptide-derived piperazinones containing an aromatic urea moiety and a basic amino acid has been synthesized and evaluated as inhibitors of human platelet aggregation induced by the PAR1 agonist SFLLRN and as cytotoxic agents in human cancer cells. The synthetic strategy involves coupling of a protected basic amino acid benzyl amide to 1,2- and 1,2,4-substituted-piperazinone derivatives, through a carbonylmethyl group at the N1-position, followed by formation of an aromatic urea at the exocyclic moiety linked at the C2 position of the piperazine ring and removal of protecting groups. None of the compounds showed activity in the biological evaluation.

Lysine-specific demethylase 1-selective inactivators: Protein-targeted drug delivery mechanism

Drug drop off: Given that lysine-specific demethylase 1 (LSD1) could be potently and selectively inactivated by delivering phenylcyclopropylamine (PCPA), a weak and nonselective LSD1 inhibitor, directly to the enzyme's active site, a novel series of LSD1 inactivators (1) were designed. Biological and mechanistic studies indicate that 1 inhibits LSD1 potently and selectively. Copyright

Design, synthesis and preliminary activity evaluation of novel L-lysine derivatives as aminopeptidase N/CD13 inhibitors

A novel class of L-lysine derivatives as aminopeptidase N (APN) inhibitors was designed and synthesized. Activity evaluation showed that compound C7 (IC50 = 9.6 ± 1.3 μM) and C20 (IC50 = 13.6 ± 1.9 μM) were equivalent to the positive control Bestatin (IC50 = 11.3 ± 1.6 μM).

BIOLOGICALLY POTENT ANALOGUES OF THE DMT-TIC PHARMACOPHORE AND METHODS OF USE

Disclosed are compounds of formula (I) or pharmaceutically acceptable salts thereof: formula (I) in which R1, R2, and R3 are described herein. Also disclosed is a pharmaceutical composition comprising at least one compound of formula (I) and a pharmaceutically acceptable carrier. Also disclosed is a method of agonizing or antagonizing a μ-opioid or δ-opioid receptor in a mammal in need thereof.

Effect of lysine at C-terminus of the Dmt-Tic opioid pharmacophore

Substitution of Gly with side-chain-protected or unprotected Lys in lead compounds containing the opioid pharmacophore Dmt-Tic [H-Dmt-Tic-Gly-NH-CH 2-Ph, μ agonist/δ antagonist; H-Dmt-Tic-Gly-NH-Ph, μ agonist/δ agonist; and H-Dmt-Tic-NH-CH2-Bid, δ agonist (Bid = 1H-benzimidazole-2-yl)] yielded a new series of compounds endowed with distinct pharmacological activities. Compounds (1-10) included high δ- (Kiδ = 0.068-0.64 nM) and δ-opioid affinities (Kiμ = 0.13-5.50 nM), with a bioactivity that ranged from μ-opioid agonism {10, H-Dmt-Tic-NH-CH[(CH2) 4-NH2]-Bid (IC50 GPI = 39.7 nM)} to a selective μ-opioid antagonist [3, H-Dmt-Tic-Lys-NH-CH2-Ph (pA 2μ = 7.96)] and a selective δ-opioid antagonist [5, H-Dmt-Tic-Lys(Ac)-NH-Ph (pA2δ = 12.0)]. The presence of a Lys linker provides new lead compounds in the formation of opioid peptidomimetics containing the Dmt-Tic pharmacophore with distinct agonist and/or antagonist properties.

Synthesis of benzylamides of dipeptides as potential inhibitors of plasmin

Four benzylamides of dipeptides with the general formula: X-L-Lys-NH-CH2-C6H5, where X = L-or D-Leu and L-or D-Phe were prepared as potential inhibitors of plasmin. All of them influenced on the fibrynolytic activity of plasmin, but only D-Leu-L-Lys-NH-CH2-C6H5 inhibited the amidolytic activity of this enzyme. None of the tested compounds was an inhibitor of thrombin in an amidolytic test.