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Highly Potent, Stable, and Selective Dimeric Hetarylpropylguanidine-Type Histamine H2 Receptor Agonists
Pockes, Steffen
, Wifling, David
, Keller, Max, Buschauer, Armin
und Elz, Sigurd
(2018)
Highly Potent, Stable, and Selective Dimeric Hetarylpropylguanidine-Type Histamine H2 Receptor Agonists.
ACS Omega 2018 (3), S. 2865-2882.
Veröffentlichungsdatum dieses Volltextes: 14 Mai 2018 13:57
Artikel
DOI zum Zitieren dieses Dokuments: 10.5283/epub.37314
Zusammenfassung
On the basis of the long-known prototypic pharmacophore 3-(1H-imidazol-4-yl) propylguanidine (SK&F 91486, 2), monomeric, homodimeric, and heterodimeric bisalkylguanidine-type histamine H-2 receptor (H2R) agonists with various alkyl spacers were synthesized. Aiming at increased H2R selectivity of the ligands, the imidazol-4-yl moiety was replaced by imidazol-1-yl, 2-aminothiazol-5-yl or ...
On the basis of the long-known prototypic pharmacophore 3-(1H-imidazol-4-yl) propylguanidine (SK&F 91486, 2), monomeric, homodimeric, and heterodimeric bisalkylguanidine-type histamine H-2 receptor (H2R) agonists with various alkyl spacers were synthesized. Aiming at increased H2R selectivity of the ligands, the imidazol-4-yl moiety was replaced by imidazol-1-yl, 2-aminothiazol-5-yl or 2-amino-4-methylthiazol-5-yl according to a bioisosteric approach. All compounds turned out to be partial or full agonists at the h/gp/rH(2)R. The most potent analogue, the thiazole-type heterodimeric ligand 63 (UR-Po461), was a partial agonist (E-max = 88%) and 250 times more potent than histamine (pEC(50): 8.56 vs 6.16, gpH(2)R, atrium). The homodimeric structures 56 (UR-Po395) and 58 (UR-Po448) exhibited the highest hH(2)R affinities (pK(i): 7.47, 7.33) in binding studies. Dimeric amino(methyl) thiazole derivatives, such as 58, generated an increased hH(2)R selectivity compared to the monomeric analogues, e.g., 139 (UR-Po444). Although monomeric ligands showed up lower affinities and potencies at the H2R, compounds with a short alkylic side chain like 129 (UR-Po194) proved to be highly affine hH(4)R ligands.
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| Dokumentenart | Artikel | ||||
| Titel eines Journals oder einer Zeitschrift | ACS Omega | ||||
| Verlag: | American Chemical Society | ||||
|---|---|---|---|---|---|
| Ort der Veröffentlichung: | WASHINGTON | ||||
| Band: | 2018 | ||||
| Nummer des Zeitschriftenheftes oder des Kapitels: | 3 | ||||
| Seitenbereich: | S. 2865-2882 | ||||
| Datum | März 2018 | ||||
| Zusätzliche Informationen (Öffentlich) | zu den Nachnutzungsbedingungen: "ACS AuthorChoice - This is an open access article published under an ACS AuthorChoice License (https://pubs.acs.org/page/policy/authorchoice_termsofuse.html), which permits copying and redistribution of the article or any adaptations for non-commercial purposes | ||||
| Institutionen | Chemie und Pharmazie > Institut für Pharmazie > Lehrstuhl Pharmazeutische / Medizinische Chemie I (Prof. Elz) | ||||
| Identifikationsnummer |
| ||||
| Stichwörter / Keywords | G-ACYLATED IMIDAZOLYLPROPYLGUANIDINES; HIGH CONSTITUTIVE ACTIVITY; PROTEIN-COUPLED RECEPTORS; IN-VITRO PHARMACOLOGY; H-4 RECEPTOR; MOLECULAR-DYNAMICS; BINDING-SITE; SF9; SYNCHRONIZATION; ANTAGONIST; | ||||
| Dewey-Dezimal-Klassifikation | 500 Naturwissenschaften und Mathematik > 540 Chemie 600 Technik, Medizin, angewandte Wissenschaften > 615 Pharmazie | ||||
| Status | Veröffentlicht | ||||
| Begutachtet | Ja, diese Version wurde begutachtet | ||||
| An der Universität Regensburg entstanden | Ja | ||||
| URN der UB Regensburg | urn:nbn:de:bvb:355-epub-373145 | ||||
| Dokumenten-ID | 37314 |
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