Design, Synthesis, and Biological Activities of Four Angiotensin II Receptor Ligands with γ-Turn Mimetics Replacing Amino Acid Residues 3−5

1997 ◽  
Vol 40 (6) ◽  
pp. 903-919 ◽  
Author(s):  
Boris Schmidt ◽  
Susanna Lindman ◽  
Weimin Tong ◽  
Gunnar Lindeberg ◽  
Adolf Gogoll ◽  
...  
Keyword(s):  
Amino Acid ◽  
Angiotensin Ii ◽  
Biological Activities ◽  
Amino Acid Residues ◽  
Angiotensin Ii Receptor ◽  
Receptor Ligands ◽  
Design Synthesis

Analogues of the cholecystokinin octapeptide modified in the central part of the molecule

1991 ◽  
Vol 56 (9) ◽  
pp. 1963-1970 ◽  
Author(s):  
Jan Hlaváček ◽  
Václav Čeřovský ◽  
Jana Pírková ◽  
Pavel Majer ◽  
Lenka Maletínská ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Point Of View ◽  
Biologically Active ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Cholecystokinin Octapeptide ◽  
Biological Tests ◽  
Biological Potency ◽  
Biologically Active Conformation

In a series of analogues of the cholecystokinin octapeptide (CCK-8) the amino acid residues were gradually modified by substituting Gly by Pro in position 4, Trp by His in position 5, Met by Cle in position 6, or the Gly residue was inserted between Tyr and Met in positions 2 and 3 of the peptide chain, and in the case of the cholecystokinin heptapeptide (CCK-7) the Met residues were substituted by Nle or Aib. These peptides were investigated from the point of view of their biological potency in the peripheral and central region. From the results of the biological tests it follows that the modifications carried out in these analogues and in their Nα-Boc derivatives mean a suppression of the investigated biological activities by 2-3 orders of magnitude (at a maximum dose of the tested substance of 2 . 10-2 mg per animal).This means that a disturbance of the assumed biologically active conformation of CCK-8, connected with a considerable decrease of the biological potency of the molecule, takes place not only after introduction of the side chain into its centre (substitution of Gly4), but also after the modification of the side chains of the amino acids or by extension of the backbone in further positions around this central amino acid.

Synthesis of Fragments of the Vasoactive Intestinal Peptide (VIP) and Analysis of Their Residual Biological Activities

1995 ◽  
Vol 60 (7) ◽  
pp. 1229-1235 ◽  
Author(s):  
Ivana Zoulíková ◽  
Ivan Svoboda ◽  
Jiří Velek ◽  
Václav Kašička ◽  
Jiřina Slaninová ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Residual Activity ◽  
Detailed Examination ◽  
Amino Acid Residues ◽  
Linear Peptide ◽  
Zone Electrophoresis ◽  
Capillary Zone

The vasoactive intestinal (poly)peptide (VIP) is a linear peptide containing 28 amino acid residues, whose primary structure indicates a low metabolic stability. The following VIP fragments, as potential metabolites, and their analogues were prepared by synthesis on a solid: [His(Dnp)1]VIP(1-10), VIP(11-14), [D-Arg12]VIP(11-14), [Lys(Pac)15,21,Arg20]VIP(15-22), and VIP(23-28). After purification, the peptides were characterized by amino acid analysis, mass spectrometry, RP HPLC, and capillary zone electrophoresis. In some tests, detailed examination of the biological activity of the substances in vivo and in vitro gave evidence of a low, residual activity of some fragments, viz. a depressoric activity in vivo for [His(Dnp)1]VIP(1-10) and a stimulating activity for the release of α-amylase in vitro and in vivo for [Lys(Pac)15,21,Arg20]VIP(15-22) and VIP(23-28).

scholarly journals Design, synthesis and evaluation of novel angiotensin II receptor 1 antagonists with antihypertensive activities

RSC Advances ◽  
2017 ◽  
Vol 7 (42) ◽  
pp. 26401-26410 ◽  
Author(s):  
Xiao-Lu Bao ◽  
Wei-Bo Zhu ◽  
Tian-Li Shan ◽  
Zhuo Wu ◽  
Rui-Jing Zhang ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Antihypertensive Drug ◽  
Drug Candidate ◽  
Ang Ii ◽  
Angiotensin Ii Receptor ◽  
Design Synthesis ◽  
Long Acting

A novel Ang II receptor 1 antagonist 1f was found to be an efficient, long-acting and safe antihypertensive drug candidate.

ChemInform Abstract: PHOTOAFFINITY LABELING OF THE ANGIOTENSIN II RECEPTOR. PART 1. SYNTHESIS AND BIOLOGICAL ACTIVITIES OF THE LABELING PEPTIDES

1979 ◽  
Vol 10 (8) ◽  
Author(s):  
E. H. F. ESCHER ◽  
THI MAI DUNG NGUYEN THI MAI DUNG NGUYEN ◽  
H. ROBERT ◽  
S. A. ST-PIERRE ◽  
D. C. REGOLI
Keyword(s):  
Angiotensin Ii ◽  
Biological Activities ◽  
Photoaffinity Labeling ◽  
Angiotensin Ii Receptor

Design, synthesis, and evaluation of novelly substituted benzimidazole compounds as angiotensin II receptor antagonists

2005 ◽  
Vol 15 (17) ◽  
pp. 3962-3965 ◽  
Author(s):  
Alka Bali ◽  
Yogita Bansal ◽  
M. Sugumaran ◽  
Jatinder Singh Saggu ◽  
P. Balakumar ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Angiotensin Ii Receptor ◽  
Angiotensin Ii Receptor Antagonists ◽  
Receptor Antagonists ◽  
Design Synthesis

Cyclic mu-opioid receptor ligands containing multiple N -methylated amino acid residues

2017 ◽  
Vol 27 (8) ◽  
pp. 1644-1648 ◽  
Author(s):  
Anna Adamska-Bartłomiejczyk ◽  
Anna Janecka ◽  
Márton Richárd Szabó ◽  
Maria Camilla Cerlesi ◽  
Girolamo Calo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Opioid Receptor ◽  
Mu Opioid Receptor ◽  
Amino Acid Residues ◽  
Receptor Ligands ◽  
Mu Opioid ◽  
Opioid Receptor Ligands

Photoaffinity labeling of the angiotensin II receptor; pharmacology of the labeling peptides in the dark

1978 ◽  
Vol 56 (6) ◽  
pp. 956-962 ◽  
Author(s):  
E. Escher ◽  
T. M. D. Nguyen ◽  
D. Regoli
Keyword(s):  
Angiotensin Ii ◽  
Biological Activities ◽  
Photoaffinity Labeling ◽  
Rabbit Aorta ◽  
Competitive Inhibitor ◽  
Current View ◽  
Angiotensin Ii Receptor ◽  
Aromatic Side Chain ◽  
Receptor Pharmacology ◽  
Measurable Activity

The biological activities of photoaffinity labeling analogs of angiotensin II (ATII) and their precursors were measured in rabbit aorta strips in the dark. Most of the analogs behave as reversible, specific agonists, one as a competitive inhibitor. The activities are discussed in line with the current view of structural requirements. The modifications consisted of substitutions on the aromatic nuclei of Tyr4 and Phe8 in [Sar1]ATII with (4′-NO2)Phe, (4′-NH2)Phe, (4′-N3)Phe, (4′-N2+)Phe, and (4′-NH2-3′, 5′-I2)Phe. It is shown that the affinity of the ATII analogs modified in position 4 depends on the electronegativity and not on space-filling properties of the aromatic residue; rising electronegativity lowers the affinity, i.e., [Sar1, (4′-NO2)Phe4]ATII has no more measurable activity. Substituting the aromatic side chain in position 8 of [Sar1]ATII gives well-binding analogs with intrinsic activities from 0 to 100% and activity seems to depend only on stereochemical requirements. Agonists and partial agonists bear rather small groups like -NH2, -N3, -NO2, and -N2+. The only antagonist [Sar1, (4′-NH2-3′,5′-I2)Phe8]ATII resembles the antagonist [Sar1, Leu8]ATII in competitivity and binding.

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