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Miyata, A., Jiang, L., Dahl, R.D., Kitada, C., Kubo, K., Fujino, M., Minamino, N. and Arimura, A. (1990) Isolation of a Neuropeptide Corresponding to the N-Terminal 27 Residue of the Pituitary Adenylate Cyclase Activating Polypeptide with 38 Residue (PACAP38). Biochemical and Biophysical Research Communications, 170, 643-648. http://dx.doi.org/10.1016/0006-291X(90)92140-U

has been cited by the following article:

• TITLE: Potential PET Ligands for Imaging of Cerebral VPAC and PAC Receptors: Are Non-Peptide Small Molecules Superior to Peptide Compounds?

  AUTHORS: Margit Pissarek

  KEYWORDS: Class B Receptors, Vasoactive Intestinal Peptide, Pituitary Adenylate Cyclase Activating Polypeptide, Non-Peptide Ligands, PET, SPECT

  JOURNAL NAME: World Journal of Neuroscience, Vol.5 No.5, November 17, 2015

  ABSTRACT: Pituitary adenylate cyclase activating polypeptide (PACAP) and vasoactive intestinal peptide (VIP) have been known for decades to mediate neuroendocrine and vasodilative actions via G-protein-coupled receptors of Class B. These are targets of imaging probes for positron emission tomography (PET) or single photon emission tomography (SPECT) in tumor diagnostics and tumor grading. However, they play only a subordinate role in the development of tracers for brain imaging. Difficulties in development of non-peptide ligands typical for cerebral receptors of PACAP and VIP are shared by all members of Class B receptor family. Essential landmarks have been confirmed for understanding of structural details of Class B receptor molecular signalling during the last five years. High relevance in the explanation of problems in ligand development for these receptors is admitted to the large N-terminalectodomain markedly different from Class A receptor binding sites and poorly suitable as orthosteric binding sites for the most small-molecule compounds. The present study is focused on the recently available receptor ligands for PAC1, VPAC1 and VPAC2 receptors as well as potential small-molecule lead structures suitable for use in PET or SPECT. Recently, biaryl, cyanothiophene and pentanamide structures with affinities in nM-range have been proposed as non-peptide ligands at VPAC1 and VPAC2 receptors. However, most of these ligands have been classified as non-competitive related to the orthosteric binding site of endogenous peptide ligands of VPAC receptors. For PAC1 receptors have been identified hydrazide compounds for which an inhibitory and potentially competitive mechanism of receptor binding has been postulated based on molecular docking studies.