Synthesis and some pharmacological properties of [2-tryptophan]-oxytocin

1976 ◽  
Vol 54 (5) ◽  
pp. 512-516 ◽  
Author(s):  
B. M. Ferrier ◽  
L. A. Branda
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Aromatic Amino Acid ◽  
Biological Activities ◽  
Pharmacological Properties ◽  
Milk Ejection ◽  
Aromatic Amino Acid Residue

Previous studies have suggested that an aromatic amino acid residue at position 2 in oxytocin facilitates the expression of the hormone's biological activities. [2-Tryptophan]-oxytocin, in which a residue of tryptophan has replaced that of tyrosine in oxytocin, has been synthesized by the method of azide coupling of the N-terminal dipeptide and C-terminal heptapeptide amide. It was found to have approximately 0.1% of the potency of oxytocin in milk ejection and uterotonic biological activities.

Local stability identification and the role of a key aromatic amino acid residue in staphylococcal nuclease refolding

FEBS Journal ◽  
2005 ◽  
Vol 272 (15) ◽  
pp. 3960-3966 ◽  
Author(s):  
Zhengding Su ◽  
Jiun-Ming Wu ◽  
Huey-Jen Fang ◽  
Tian-Yow Tsong ◽  
Hueih-Min Chen
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Aromatic Amino Acid ◽  
Local Stability ◽  
Staphylococcal Nuclease ◽  
Aromatic Amino Acid Residue

scholarly journals THE ACTION OF CRYSTALLINE PROTEOLYTIC ENZYMES ON ANGIOTONIN

1944 ◽  
Vol 79 (2) ◽  
pp. 205-214 ◽  
Author(s):  
Albert A. Plentl ◽  
Irvine H. Page
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Aromatic Amino Acid ◽  
Proteolytic Enzymes ◽  
Basic Amino Acid ◽  
Enzymatic Digestion ◽  
Carboxyl Group ◽  
Peptide Linkage ◽  
Aromatic Amino Acid Residue

Angiotonin was subjected to enzymatic digestion by crystalline carboxy-peptidase, chymotrypsin, trypsin, and pepsin. These enzymes were found to destroy it in vitro. Hydrogen ion optima and proteolytic coefficients for these reactions were determined and were found to be of approximately the expected magnitude for typical substrates. Regarding the purified crystalline enzymes as reagents, the experimental findings were interpreted on the basis of Bergmann's specificity studies. We were thus directed to the conclusion that angiotonin contains (1) a free terminal amino group, (2) a free terminal carboxyl group, (3) one basic amino acid residue which may be terminal but its carboxyl must be united in a peptide linkage, (4) one central dibasic amino acid residue in combination with an aromatic amino acid residue, (5) an aromatic amino acid residue which may be part of (4) and, if not part of (4) must be terminal with its carboxyl group in peptide linkage. The simplest compound satisfying these conditions is tyrosyl-arginylglutamyl-phenylalanine or a combination of amino acids with similar general characteristics.

scholarly journals Exploring cucurbit[6]uril–peptide interactions in the solid state: crystal structure of cucurbit[6]uril complexes with glycyl-containing dipeptides

CrystEngComm ◽  
2017 ◽  
Vol 19 (28) ◽  
pp. 3892-3897 ◽  
Author(s):  
Oksana Danylyuk
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Solid State ◽  
Amino Acid Residue ◽  
Aromatic Amino Acid ◽  
Supramolecular Complexes ◽  
Peptide Interactions ◽  
Aromatic Amino Acid Residue

Macrocyclic host cucurbit[6]uril forms supramolecular complexes with dipeptides sequenced as Gly-X, where X is either an aromatic amino acid residue Phe, Tyr, and Trp or Gly in the solid state.

Plasma Oxytocinase: The Synthesis and Biological Properties of the First Prodoct of the Degradation of Oxytocin by this Enzyme

1974 ◽  
Vol 52 (1) ◽  
pp. 60-66 ◽  
Author(s):  
B. M. Ferrier ◽  
J. M. Hendrie ◽  
L. A. Branda
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Pregnant Women ◽  
Amino Acid Residue ◽  
Biological Properties ◽  
Milk Ejection ◽  
Terminal Amino Acid ◽  
Molecular Features ◽  
Marked Inhibition ◽  
Terminal Amino

Oxytocin is hydrolytically cleaved in the presence of plasma oxytocinase to give an acyclic peptide, tyrosyl-isoleucyl-glutaminyl-asparaginyl-S-(S-cysteine)-cysteinyl-prolyl-leucyl-glycinamide (1,2-acyclic oxytocin). The synthesis of this peptide is described. It is shown to be of very low potency in milk-ejection-like activity and uterotonic activity. It does not inhibit the expression of these activities by oxytocin, suggesting that it does not interfere with the hormone's binding to target tissues. The presence of 1,2-acyclic oxytocin slightly inhibits the rate of degradation of oxytocin by plasma from pregnant women, in contrast to the marked inhibition of the degradation of cystine di-β-naphthylamide. The Km for the degradation of oxytocin is 30 times smaller than that of the degradation of cystine di-β-naphthylamide, which is of the same order as the Ki for the inhibition of the degradation of cystine di-β-naphthylamide by 1,2-acyclic oxytocin. These results, together with information on the substrate specificity of plasma oxytocinase with respect to the N-terminal amino acid residue, suggest that there are molecular features of oxytocin other than its N-terminal residue that facilitate its interaction with plasma oxytocinase.

Design and Molecular Docking Studies of Some 2,3 Di-Substituted Quinazolin-4-One Analogues Against Staphylococcus aureus UDG

2020 ◽  
Vol 16 (4) ◽  
pp. 402-406
Author(s):  
Amrute B. Bhavesh ◽  
Amrutkar D. Rakesh ◽  
Tambe R. Santosh
Keyword(s):  
Staphylococcus Aureus ◽  
Hydrogen Bond ◽  
Molecular Docking ◽  
Amino Acid ◽  
Amino Acid Residue ◽  
Broad Spectrum ◽  
Biological Activities ◽  
Docking Studies ◽  
Pharmaceutical Chemistry ◽  
Diverse Range

Background: In this present investigation, some 2, 3 disubstituted-quinazolin-4-one derivatives are designed and docked against chain A and chain B of (3WDF) receptor. Methods: The heterocyclic fused rings quinazolinone have drawn a great attention owing to their expanded applications in the field of pharmaceutical chemistry. The diverse range of molecules with quinazoline/quinazolinone moieties have been reported to exhibit a broad spectrum of biological activities. Results: The results designate that the quinazolinone ring forms hydrophobic and hydrogen bond contacts with ASN 127 A, ALA 126 A, and SER 83 B, SER 183 B amino acid residue. Conclusion: : Molecular docking is safe and straightforward to use tool which facilitates in investigating, interpreting, enplaning and identification of molecular properties using 3D structures.

scholarly journals PHYTOHEMAGGLUTININ MITOGENIC PROTEINS

1973 ◽  
Vol 138 (4) ◽  
pp. 939-951 ◽  
Author(s):  
J. Bruce Miller ◽  
Claudia Noyes ◽  
Robert Heinrikson ◽  
Henry S. Kingdon ◽  
Stanley Yachnin
Keyword(s):  
Amino Acid ◽  
Phaseolus Vulgaris ◽  
Amino Acid Residue ◽  
Primary Structure ◽  
Biological Activities ◽  
Amino Acid Sequences ◽  
Structural Basis ◽  
Amino Terminal ◽  
Isoelectric Points

The phytohemagglutinin (PHAP) glycoproteins derived from Phaseolus vulgaris consist of five isomitogens that are tetrameric structures made up of two different glycoprotein subunits. Although identical in size (mol wt = 34,000), the subunits differ in their isoelectric points and amino acid sequences for six of the first seven amino-terminal residues, but are identical in primary structure from the 8th through the 24th amino acid residue. The isomitogen containing four L subunits (L-PHAP) is a potent leukoagglutinin and mitogen that lacks hemagglutinating properties. The isomitogen made up of four R subunits (4R H-PHAP) is a potent hemagglutinin. The hybrid isomitogens consisting of varying proportions of the two subunits (3L-1R, 2L-2R, 1L-3R) are capable of causing mixed erythrocyte-lymphocyte agglutination. These studies provide a structural basis for explaining the differences in biological activities of the various PHAP isomitogens.

Influence of C-Terminal Modifications of Bradykinin Antagonists on Their Activity

1997 ◽  
Vol 62 (12) ◽  
pp. 1940-1946 ◽  
Author(s):  
Adam Prahl ◽  
Tomasz Wierzba ◽  
Pawel Winklewski ◽  
Magdalena Wszedybyl ◽  
Maciej Cherek ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Pharmacological Properties ◽  
Terminal Part ◽  
Conscious Rats ◽  
Bradykinin Antagonists ◽  
Vasodepressor Response

In the present study we have described the synthesis and some pharmacological properties of four new analogues of bradykinin (BK). Two peptides were designed by substitution of positions 7 and 8 of known B2 antagonists with N-methyl-L-phenylalanine [Phe(Me)]. The next two analogues were obtained by replacement of D-Phe residue in position 7 of known B2 antagonist with 1-naphthyl-D-alanine or 2-naphthyl-D-alanine. The antagonistic potency of peptides was assessed by their ability to inhibit vasodepressor response to exogenous bradykinin in conscious rats. Although our studies demonstrated disadvantegous influence of Phe(Me)7,8 modification for B2 antagonism, we showed that D-amino acid residue in position 7 of BK antagonists may be replaced by suitable L-amino acid residue. As regards (D-Nal)7 substitution, we found strikingly different antagonistic potencies of analogues which differ only in the presence of D-1-Nal and D-2-Nal. We assume that it is due to different conformations of these peptides, proving the importance of the shape of the C-terminal part of B2 antagonists for their activity.

Predicting the Strength of Stacking Interactions Between Heterocycles and Aromatic Amino Acid Side Chains

2019 ◽  
Author(s):  
Andrea N. Bootsma ◽  
Analise C. Doney ◽  
Steven Wheeler
Keyword(s):  
Amino Acid ◽  
Binding Sites ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acids ◽  
Biologically Active ◽  
Side Chains ◽  
Stacking Interactions ◽  
Inhibitor Binding ◽  
Protein Binding Sites ◽  
Amino Acid Side Chains

<p>Despite the ubiquity of stacking interactions between heterocycles and aromatic amino acids in biological systems, our ability to predict their strength, even qualitatively, is limited. Based on rigorous <i>ab initio</i> data, we have devised a simple predictive model of the strength of stacking interactions between heterocycles commonly found in biologically active molecules and the amino acid side chains Phe, Tyr, and Trp. This model provides rapid predictions of the stacking ability of a given heterocycle based on readily-computed heterocycle descriptors. We show that the values of these descriptors, and therefore the strength of stacking interactions with aromatic amino acid side chains, follow simple predictable trends and can be modulated by changing the number and distribution of heteroatoms within the heterocycle. This provides a simple conceptual model for understanding stacking interactions in protein binding sites and optimizing inhibitor binding in drug design.</p>

Pharmacologically potentials of different substituted coumarin derivatives

2019 ◽  
Author(s):  
Chem Int
Keyword(s):  
Benzene Ring ◽  
Bioactive Compounds ◽  
Biological Activities ◽  
Pharmacological Properties ◽  
Coumarin Derivatives ◽  
Wide Range ◽  
Anti Oxidant ◽  
Anti Inflammatory ◽  
Coumarin Compounds

Coumarin and its derivatives are widely spread in nature. Coumarin goes to agroup as benzopyrones, which consists of a benzene ring connected to a pyronemoiety. Coumarins displayed a broad range of pharmacologically useful profile.Coumarins are considered as a promising group of bioactive compounds thatexhibited a wide range of biological activities like anti-microbial, anti-viral,antiparasitic, anti-helmintic, analgesic, anti-inflammatory, anti-diabetic, anticancer,anti-oxidant, anti-proliferative, anti-convulsant, and antihypertensiveactivities etc. The coumarin compounds have immense interest due to theirdiverse pharmacological properties. In particular, these biological activities makecoumarin compounds more attractive and testing as novel therapeuticcompounds.

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