120230-41-3Relevant academic research and scientific papers
Structure-Based Discovery of Proline-Derived Arginase Inhibitors with Improved Oral Bioavailability for Immuno-Oncology
Lu, Min,Zhang, Hongjun,Li, Derun,Childers, Matthew,Pu, Qinglin,Palte, Rachel L.,Gathiaka, Symon,Lyons, Thomas W.,Palani, Anandan,Fan, Peter W.,Spacciapoli, Peter,Miller, J. Richard,Cho, Hyelim,Cheng, Mangeng,Chakravarthy, Kalyan,O'Neil, Jennifer,Eangoor, Padmanabhan,Beard, Adam,Kim, Hai-Young,Saurí, Josep,Gunaydin, Hakan,Sloman, David L.,Siliphaivanh, Phieng,Cumming, Jared,Fischer, Christian
, p. 1380 - 1388 (2021)
Recent data suggest that the inhibition of arginase (ARG) has therapeutic potential for the treatment of a number of indications ranging from pulmonary and vascular disease to cancer. Thus, high demand exists for selective small molecule ARG inhibitors wi
ARGINASE INHIBITORS AND METHODS OF USE
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, (2019/10/04)
Described herein are compounds of Formula I or a pharmaceutically acceptable salt thereof. The compounds of Formula I act as arginase inhibitors and can be useful in preventing, treating or acting as a remedial agent for arginase-related diseases.
Native chemical ligation at valine: A contribution to peptide and glycopeptide synthesis
Chen, Jin,Wan, Qian,Yuan, Yu,Zhu, Jianglong,Danishefsky, Samuel J.
supporting information; experimental part, p. 8521 - 8524 (2009/05/07)
(Chemical Equation Presented) A Val-uable link: The title transformation is achieved by a two-step ligation, radicalbased desulfurization strategy (see scheme; NCL=native chemical ligation). After S→N acyl transfer, in which the acyl acceptor is a γ-thiol valine derivative, and site-specific dethiolation, a valine residue appears at the site of ligation. This method accomplishes ligations at Thr-Val and Pro-Val sites, and allows successful ligation of glycopeptide fragments.
An olefination entry for the synthesis of enantiopure α,ω-diaminodicarboxylates and azabicyclo[X.Y.0]alkane amino acids
Gosselin, Francis,Lubell, William D.
, p. 7463 - 7471 (2007/10/03)
A new approach for synthesizing α,ω-diaminodicarboxylates of various chain lengths has opened the way for making a series of azabicyclo[X.Y.0]alkane amino acids of different ring sizes. β-Keto phosphonates 21-23 were synthesized in 71-90% yield by the addition of the lithium anion of dimethyl methyl phosphonate to the ω-methyl ester of α.-tert-butyl N-(PhF)aspartate 3, glutamate 9, and aminoadipate 12 (PhF = 9-phenylfluoren-9-yl). α,ω-Diaminodicarboxylates 24-26 of nine to eleven carbon chain lengths were prepared in 78-87% yield from the Horner-WadsworthEmmons olefination of α-tert-butyl .ZV-(PhF)aspartatc β-aldehyde (5) with aminodicarboxylate-derived β-keto phosphonates 21-23. The power of this approach for making azabicyclo[X.Y.0]alkane amino acid was then illustrated by the first synthesis of enantiopure indolizidin-9-one amino acid 2 in nine steps and >25% overall yield from inexpensive aspartic acid as chiral educt. Hydrogenation of (2S,8S)-di-tcrt-butyl 4-oxo-2,8-bis[N-(PhF)amino]non-4-enedioate (24) in 9:1 EtOH:AcOH furnished a 9:1 diastereomeric mixture of 6-alkylpipecolate 28 that was subsequently transformed into azabicyclo[4.3.0]alkane amino acid 2 via lactam cyclization and protecting group manipulations. Because α,ω-diaminodicarboxylates 25 and 26 may be similarly converted to heterocycles of larger ring sizes and because alkylation of similar ketones can be used to attach side-chains at different points on the heterocycle, this olefination strategy greatly expands our methodology for synthesizing azabicyclo[X.Y.0]alkane amino acids for the exploration of conformation-activity relationships of various biologically active peptides.
