6281-32-9Relevant articles and documents
A second generation photochemically activatable dynemicin analog: A concise synthesis and DNA cleavage studies
Wender,Beckham,O'Leary
, p. 1278 - 1282 (1994)
A scheme for the design of dynemicin analogs and a concise, efficient route for their synthesis are described. A photochemically activatable analog was prepared and shown to undergo cycloaromatization upon irradiation with wavelengths greater than 300 nm. The ability of this compound to function as a competent DNA cleaving agent is demonstrated.
Hydroxymethylation of quinolinesviairon promoted oxidative C-H functionalization: synthesis of arsindoline-A and its derivatives
Shantharjun, Bangarigalla,Vani, Damera,Unnava, Ramanjaneyulu,Sandeep, Mummadi,Reddy, Kallu Rajender
, p. 645 - 652 (2021/02/06)
Herein, we report a mild and efficient hydroxymethylation of quinolinesviaan iron promoted cross-dehydrogenative coupling reaction under external acid free conditions. Various hydroxyalkyl substituted quinolines were achieved in excellent yields with well tolerated functional groups. Importantly, a few of the hydroxylmethylated quinolines were further transformed into respective aldehydes, and were successfully utilized for the synthesis of alkaloid arsindoline-A and its derivatives.
AMINOPYRAZINE COMPOUNDS AS HPK1 INHIBITOR AND THE USE THEREOF
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Page/Page column 61, (2021/02/26)
Disclosed herein is an aminopyrazine compound of Formula (I), or a stereoisomer thereof, or a pharmaceutically acceptable salt thereof, and pharmaceutical compositions comprising thereof. Also disclosed is a method of treating HPK1 related disorders or diseases by using the compound disclosed herein.
Synthesis and Biological Evaluation of Hapten-Clicked Analogues of The Antigenic Peptide Melan-A/MART-126(27L)-35
Tarbe, Marion,Miles, John J.,Edwards, Emily S. J.,Miles, Kim M.,Sewell, Andrew K.,Baker, Brian M.,Quideau, Stéphane
supporting information, p. 799 - 807 (2020/04/20)
A click-chemistry-based approach was implemented to prepare peptidomimetics designed in silico and made from aromatic azides and a propargylated GIGI-mimicking platform derived from the altered Melan-A/MART-126(27L)-35 antigenic peptide ELAGIGILTV. The CuI-catalyzed Huisgen cycloaddition was carried out on solid support to generate rapidly a first series of peptidomimetics, which were evaluated for their capacity to dock at the interface between the major histocompatibility complex class-I (MHC-I) human leucocyte antigen (HLA)-A2 and T-cell receptors (TCRs). Despite being a weak HLA-A2 ligand, one of these 11 first synthetic compounds bearing a p-nitrobenzyl-triazole side chain was recognized by the receptor proteins of Melan-A/MART-1-specific T-cells. After modification of the N and C termini of this agonist, which was intended to enhance HLA-A2 binding, one of the resulting seven additional compounds triggered significant T-cell responses. Thus, these results highlight the capacity of naturally circulating human TCRs that are specific for the native Melan-A/MART-126-35 peptide to cross-react with peptidomimetics bearing organic motifs structurally different from the native central amino acids.
