169448-55-9

Upstream product

• 169448-54-8 (R)-N-(tert-butoxycarbonyl)-2-amino-3-propyl-N-methoxy-N-methylpropionamide 
• 55674-63-0 (R)-2-(N-t-butoxycarbonylamino)hexanoic acid 
• 116640-17-6 tert-butyl (R)-(1-hydroxyhexan-2-yl)carbamate 

Downstream Products

• 169448-56-0 N-benzyl 2(R)-tert-butoxycarbonylaminohexyl-1-amine 

Relevant academic research and scientific papers

Inhibition of group IVA cytosolic phospholipase A2 by novel 2-oxoamides in vitro, in cells, and in vivo

The Group IVA cytosolic phospholipase A2 (GIVA PLA2) is a particularly attractive target for drug development because it is the rate-limiting provider of proinflammatory mediators. We previously reported the discovery of novel 2-oxoa

Synthesis of new (-)-bestatin-based inhibitor libraries reveals a novel binding mode in the S1 pocket of the essential malaria M1 metalloaminopeptidase

The malarial PfA-M1 metallo-aminopeptidase is considered a putative drug target. The natural product dipeptide mimetic, bestatin, is a potent inhibitor of PfA-M1. Herein we present a new, efficient, and high-yielding protocol for the synthesis of bestatin derivatives from natural and unnatural N-Boc-d-amino acids. A diverse library of bestatin derivatives was synthesized with variants at the side chain of either the α-hydroxyβ-amino acid (P1) or the adjacent naturalα-amino acid (P1′). Surprisingly, we found that extended aromatic side chains at the P1 position resulted in potent inhibition against PfA-M1. To understand these data, we determined the X-ray cocrystal structures of PfA-M1 with two derivatives having either a Tyr(OMe) 15 or Tyr(OBzl) 16 at the P1 position and observed substantial inhibitor-induced rearrangement of the primary loop within the PfA-M1 pocket that interacts with the P1 side chain. Our data provide important insights for the rational design of more potent and selective inhibitors of this enzyme that may eventually lead to new therapies for malaria.

AMIDES AS INHIBITORS OF HUMAN SECRETED PHOSPHOLIPASE A2

Methods and compounds useful for inhibiting a phoshpolipase A2 are provided, the methods comprising contacting the phoshpolipase A2 with a compound having the structure A, or pharmaceutically acceptable salts thereof: wherein R1

Structure-activity relationships of natural and non-natural amino acid-based amide and 2-oxoamide inhibitors of human phospholipase A2 enzymes

A variety of 2-oxoamides and related amides based on natural and non-natural amino acids were synthesized. Their activity on two human intracellular phospholipases (GIVA cPLA2 and GVIA iPLA2) and one human secretory phospholipase (GV

3-Amino-2-hydroxyamides and related compounds as inhibitors of methionine aminopeptidase-2

Substituted 3-amino-2-hydroxyamides and related hydroxyamides and acylhydrazines were identified as inhibitors of human methionine aminopeptidase-2 (MetAP2). Examination of substituents through parallel synthesis and iterative structure-based design allow

Novel 2-oxoamide inhibitors of human group IVA phospholipase A2

A novel class of potent human cytosolic phospholipase A2 (GIVA PLA2) inhibitors was developed. These inhibitors were designed to contain the 2-oxoamide functionality and a free carboxyl group. Among the compounds tested, a longchain

Inhibitors of farnesyl-protein transferase

The present invention is directed to compounds which inhibit farnesyl-protein transferase (FTase) and the farnesylation of the oncogene protein Ras. The invention is further directed to chemotherapeutic compositions containing the compounds of this invention and methods for inhibiting farnesyl-protein transferase and the farnesylation of the oncogene protein Ras. The compounds of formula A are representative of the compounds of the present invention: STR1