91133-59-4Relevant academic research and scientific papers
Constraining the Side Chain of C-Terminal Amino Acids in Apelin-13 Greatly Increases Affinity, Modulates Signaling, and Improves the Pharmacokinetic Profile
Tran, Kien,Van Den Hauwe, Robin,Sainsily, Xavier,Couvineau, Pierre,C?té, Jér?me,Simard, Louise,Echevarria, Marco,Murza, Alexandre,Serre, Alexandra,Théroux, Léa,Saibi, Sabrina,Haroune, Lounès,Longpré, Jean-Michel,Lesur, Olivier,Auger-Messier, Mannix,Spino, Claude,Bouvier, Michel,Sarret, Philippe,Ballet, Steven,Marsault, éric
supporting information, p. 5345 - 5364 (2021/02/16)
Side-chain-constrained amino acids are useful tools to modulate the biological properties of peptides. In this study, we applied side-chain constraints to apelin-13 (Ape13) by substituting the Pro12 and Phe13 positions, affecting the binding affinity and signaling profile on the apelin receptor (APJ). The residues 1Nal, Trp, and Aia were found to be beneficial substitutions for Pro12, and the resulting analogues displayed high affinity for APJ (Ki 0.08-0.18 nM vs Ape13 Ki 0.7 nM). Besides, constrained (d-Tic) or α,α-disubstituted residues (Dbzg; d-α-Me-Tyr(OBn)) were favorable for the Phe13 position. Compounds 47 (Pro12-Phe13 replaced by Aia-Phe, Ki 0.08 nM) and 53 (Pro12-Phe13 replaced by 1Nal-Dbzg, Ki 0.08 nM) are the most potent Ape13 analogues activating the Gα12 pathways (53, EC50 Gα12 2.8 nM vs Ape13, EC50 43 nM) known to date, displaying high affinity, resistance to ACE2 cleavage as well as improved pharmacokinetics in vitro (t1/2 5.8-7.3 h in rat plasma) and in vivo.
Poly (ADP-ribose) polymerase inhibitors, preparation method and its use
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Paragraph 0179; 0180, (2016/12/16)
The invention relates to a poly(ADP-ribose)polymerase (PARP) inhibitor, a preparation method and application thereof, specifically to a series of heterocyclic compounds with structures shown as formula (I), (IA), (IB), (IC), (ID), (IE), (IF), (IG), (IH),
Absolute configurations of tubulin inhibitors taltobulin (HTI-286) and HTI-042 characterized by X-ray diffraction analysis and NMR studies
Niu, Chuansheng,Ho, Douglas M.,Zask, Arie,Ayral-Kaloustian, Semiramis
scheme or table, p. 1535 - 1538 (2010/06/21)
The stereochemistry of the tubulin inhibitors taltobulin HTI-286 (2) and HTI-042 (3) was determined by utilizing the DPFGSE 1D NOE experiment. Single crystal X-ray diffraction analysis further confirmed the absolute configuration of these two compounds, w
Generation of iminyl copper species from α-azido carbonyl compounds and their catalytic C-C bond cleavage under an oxygen atmosphere
Chiba, Shunsuke,Zhang, Line,Ang, Gim Yean,Hui, Benjamin Wei-Qiang
supporting information; experimental part, p. 2052 - 2055 (2010/07/04)
Figure presented A copper-catalyzed reaction of α-azidocarbonyl compounds under an oxygen atmosphere is reported where nitriles are formed via C-C bond cleavage of a transient iminyl copper intermediate. The transformation is carried out by a sequence of denitrogenative formation of iminyl copper species from α-azidocarbonyl compounds and their C-C bond cleavage, where molecular oxygen (1 atm) is a prerequisite to achieve the catalytic process and one of the oxygen atoms of O2 was found to be incorporated into the β-carbon fragment as a carboxylic acid.
Compounds for treating tumors
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Page 52, (2008/06/13)
The invention provides compounds of formula (I): wherein E, A, B′, R6, R7, R8, and R9 are defined in the specification which compounds exhibit anticancer activity and are useful for treating cancer.
Probing the interaction of HTI-286 with tubulin using a stilbene analogue
Lo, Mei-Chu,Aulabaugh, Ann,Krishnamurthy, Girija,Kaplan, Joshua,Zask, Arie,Smith, Robert P.,Ellestad, George
, p. 9898 - 9899 (2007/10/03)
HTI-286 is a synthetic analogue of the natural product hemiasterlin. HTI-286 is a potent antitumor agent that induces tubulin oligomerization. To investigate the binding stoichiometry and the binding site during this ligand-induced tubulin association, we
