564482-88-8Relevant academic research and scientific papers
Structure–activity relationships of succinimidyl-Cys-C(O)-Glu derivatives with different near-infrared fluorophores as optical imaging probes for prostate-specific membrane antigen
Matsuoka, Daiko,Watanabe, Hiroyuki,Shimizu, Yoichi,Kimura, Hiroyuki,Yagi, Yusuke,Kawai, Ryoko,Ono, Masahiro,Saji, Hideo
, p. 2291 - 2301 (2018)
Prostate-specific membrane antigen (PSMA), which is overexpressed in malignant prostate cancer (PCa), is an ideal target for imaging and therapy of PCa. We previously reported a PSMA imaging probe, 800CW-SCE, based on succinimidyl-Cys-C(O)-Glu (SCE) for o
Interactions between human glutamate carboxypeptidase II and urea-based inhibitors: Structural characterization
Barinka, Cyril,Byun, Youngjoo,Dusich, Crystal L.,Banerjee, Sangeeta R.,Chen, Ying,Castanares, Mark,Kozikowski, Alan P.,Mease, Ronnie C.,Pomper, Martin G.,Lubkowski, Jacek
supporting information; experimental part, p. 7737 - 7743 (2009/12/07)
Urea-based, low molecular weight ligands of glutamate carboxypeptidase II (GCPII) have demonstrated efficacy in various models of neurological disorders and can serve as imaging agents for prostate cancer. To enhance further development of such compounds, we determined X-ray structures of four complexes between human GCPII and urea-based inhibitors at high resolution. All ligands demonstrate an invariant glutarate moiety within the S1′ pocket of the enzyme. The ureido linkage between P1 and P1′ inhibitor sites interacts with the active-site Zn12+ ion and the side chains of Tyr552 and His553. Interactions within the S1 pocket are defined primarily by a network of hydrogen bonds between the P1 carboxylate group of the inhibitors and the side chains of Arg534, Arg536, and Asn519. Importantly, we have identified a hydrophobic pocket accessory to the S1 site that can be exploited for structure-based design of novel GCPII inhibitors with increased lipophilicity.
