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

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.

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

FEBS Journal ◽

10.1111/j.1742-4658.2005.04814.x ◽

2005 ◽

Vol 272 (15) ◽

pp. 3960-3966 ◽

Cited By ~ 5

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

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

Recent Progress on Kinins ◽

10.1007/978-3-0348-7321-5_70 ◽

1992 ◽

pp. 572-581 ◽

Cited By ~ 3

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

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

Canadian Journal of Biochemistry ◽

10.1139/o76-074 ◽

1976 ◽

Vol 54 (5) ◽

pp. 512-516 ◽

Cited By ~ 1

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.

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THE ACTION OF CRYSTALLINE PROTEOLYTIC ENZYMES ON ANGIOTONIN

Journal of Experimental Medicine ◽

10.1084/jem.79.2.205 ◽

1944 ◽

Vol 79 (2) ◽

pp. 205-214 ◽

Cited By ~ 15

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.

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