426844-50-0Relevant articles and documents
SPECT imaging agent for FAP-alpha specific tumor diagnosis
-
, (2020/12/10)
The invention relates to an SPECT imaging agent for FAP-alpha specific tumor diagnosis. The imaging agent is formed by taking a micromolecular FAP-alpha inhibitor of a modified N-4-quinolyl-glycine-(2S)-cyanoproline skeleton as a precursor compound, taking 99mTc as radionuclide and taking N-tris (hydroxymethyl) methylglycine (Tricine) and triphenylphosphine tri-m-sodium sulfonate (TPPTS) as synergistic ligands. Compared with the prior art, the imaging agent has high sensitivity, more excellent in-vivo biological distribution is shown, compared with the prior art, the complex has the advantagesof higher tumor uptake and tumor/organ uptake ratio, more stable coordination property, and excellent in-vivo and in-vitro stability. Due to the obvious coordination structure characteristics of theimaging agent, a one-step marking kit technology can be used, and the imaging agent has better druggability and is suitable for industrial production and clinical popularization.
HEPATITIS B ANTIVIRAL AGENTS
-
Page/Page column 43; 44, (2017/02/09)
The present invention discloses compounds of Formula (I), or pharmaceutically acceptable salts, esters, or prodrugs thereof: which inhibit the protein(s) encoded by hepatitis B virus (HBV) or interfere with the function of the HBV life cycle of the hepati
Extended structure-activity relationship and pharmacokinetic investigation of (4-quinolinoyl)glycyl-2-cyanopyrrolidine inhibitors of fibroblast activation protein (FAP)
Jansen, Koen,Heirbaut, Leen,Verkerk, Robert,Cheng, Jonathan D.,Joossens, Jurgen,Cos, Paul,Maes, Louis,Lambeir, Anne-Marie,De Meester, Ingrid,Augustyns, Koen,Van Der Veken, Pieter
supporting information, p. 3053 - 3074 (2014/05/06)
Fibroblast activation protein (FAP) is a serine protease related to dipeptidyl peptidase IV (DPPIV). It has been convincingly linked to multiple disease states involving remodeling of the extracellular matrix. FAP inhibition is investigated as a therapeutic option for several of these diseases, with most attention so far devoted to oncology applications. We previously discovered the N-4-quinolinoyl-Gly-(2S)-cyanoPro scaffold as a possible entry to highly potent and selective FAP inhibitors. In the present study, we explore in detail the structure-activity relationship around this core scaffold. We report extensively optimized compounds that display low nanomolar inhibitory potency and high selectivity against the related dipeptidyl peptidases (DPPs) DPPIV, DPP9, DPPII, and prolyl oligopeptidase (PREP) the log D values, plasma stabilities, and microsomal stabilities of selected compounds were found to be highly satisfactory. Pharmacokinetic evaluation in mice of selected inhibitors demonstrated high oral bioavailability, plasma half-life, and the potential to selectively and completely inhibit FAP in vivo.