Bradykinin Antagonists Do Not Require a D-Aromatic Amino Acid Residue at Position 7

1992 ◽  
pp. 572-581 ◽  
Author(s):  
Raymond J. Vavrek ◽  
Lajos Gera ◽  
John M. Stewart
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acid Residue ◽  
Bradykinin Antagonists

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

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.

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.

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>

Self-assembling behaviour of a modified aromatic amino acid in competitive medium

Soft Matter ◽  
2020 ◽  
Vol 16 (28) ◽  
pp. 6599-6607 ◽  
Author(s):  
Pijush Singh ◽  
Souvik Misra ◽  
Nayim Sepay ◽  
Sanjoy Mondal ◽  
Debes Ray ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acid ◽  
Photophysical Properties ◽  
Solvent Mixture ◽  
The Self ◽  
Solvent Ratio ◽  
Self Assembling

The self-assembly and photophysical properties of 4-nitrophenylalanine (4NP) are changed with the alteration of solvent and final self-assembly state of 4NP in competitive solvent mixture and are dictated by the solvent ratio.

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