Journal of medicinal chemistry, 2009-09, Vol.52 (18), p.5612-5618
2009
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Details
- Autor(en) / Beteiligte
- Titel
- The Replacement of His(4) in Angiotensin IV by Conformationally Constrained Residues Provides Highly Potent and Selective Analogues
- Ist Teil von
- Journal of medicinal chemistry, 2009-09, Vol.52 (18), p.5612-5618
- Ort / Verlag
- Columbus, OH: American Chemical Society
- Erscheinungsjahr
- 2009
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- The histidine residue in angiotensin IV was replaced by various conformationally constrained amino acids. The substitution of the His4−Pro5 dipeptide sequence by the constrained Trp analogue Aia−Gly, in combination with β2hVal substitution at the N-terminus, provided a new stable analogue H-(R)-β2hVal-Tyr-Ile-Aia-Gly-Phe-OH (AL-40) that is a potent ligand for the Ang IV receptor IRAP and selective versus AP-N and the AT1 receptor.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0022-2623eISSN: 1520-4804DOI: 10.1021/jm900651pTitel-ID: cdi_proquest_miscellaneous_67652264
- Format
- –
- Schlagworte
- Amino Acid Sequence, Aminopeptidases - metabolism, Analytical, structural and metabolic biochemistry, Angiotensin II - analogs & derivatives, Angiotensin II - chemistry, Angiotensin II - metabolism, Animals, Azepines - chemistry, Biological and medical sciences, Biomimetics, Carboxylic Acids - chemistry, CHO Cells, Cricetinae, Cricetulus, Cystinyl Aminopeptidase - metabolism, Enzymes and enzyme inhibitors, Fundamental and applied biological sciences. Psychology, Histidine, Humans, Hydrolases, Medical sciences, Miscellaneous, Pharmacology. Drug treatments, Phenylalanine - chemistry, Protein Conformation, Receptor, Angiotensin, Type 1 - metabolism, Substrate Specificity