'Targeted' molecular diversity: design and development of non-peptide antagonists for cholecystokinin and tachykinin receptors
| Autor: | David Christopher Horwell, Martyn Clive Pritchard, Ratcliffe Giles S, Jennifer Raphy |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Indoles
Phenylalanine Drug Evaluation Preclinical Hormone antagonist Ligands chemistry.chemical_compound Hormone Antagonists Meglumine Peptide Library Animals Humans Amino Acid Sequence Peptide library Receptors Tachykinin Cholecystokinin Pharmacology Oligopeptide Dipeptide Molecular Structure Antagonist Tryptophan Small molecule chemistry Biochemistry Drug Design Receptors Cholecystokinin Tachykinin receptor Oligopeptides |
| Zdroj: | Immunopharmacology. 33(1-3) |
| ISSN: | 0162-3109 |
| Popis: | A drug design strategy to non-peptide small molecule antagonists of neuropeptides is described that targets the molecular diversity which exists in the 'privileged' data set of the physico-chemical properties represented by the side-chains of the 20 genetically encoded amino acids. The strategy is exemplified by the design of a selective and high affinity cholecystokinin CCK-A antagonist PD 140548, CCK-B antagonist CI-988 (formerly PD 134308) tachykinin NK-1 antagonist PD 154075 and NK-2 antagonist Cam-2291. The NK-3 antagonists, PD 157672 and the non-peptide PD 161182, were developed from an information-rich dipeptide library constructed from 256 N-protected dipeptides and 64 hydrophobic biased dipeptides. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect