Synthesis of Novel Potent Dipeptidyl Peptidase IV Inhibitors with Enhanced Chemical Stability:  Interplay between the N-Terminal Amino Acid Alkyl Side Chain and the Cyclopropyl Group of α-Aminoacyl-l-cis-4,5-methanoprolinenitrile-Based Inhibitors

2004 ◽  
Vol 47 (10) ◽  
pp. 2587-2598 ◽  
Author(s):  
David R. Magnin ◽  
Jeffrey A. Robl ◽  
Richard B. Sulsky ◽  
David J. Augeri ◽  
Yanting Huang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chemical Stability ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Side Chain ◽  
Alkyl Side Chain ◽  
Terminal Amino Acid ◽  
Dipeptidyl Peptidase Iv Inhibitors ◽  
Cyclopropyl Group ◽  
Terminal Amino

scholarly journals Proteins of the kidney microvillar membrane. The amphipathic form of dipeptidyl peptidase IV

1979 ◽  
Vol 179 (2) ◽  
pp. 379-395 ◽  
Author(s):  
D C Macnair ◽  
A J Kenny
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Amino Acid Sequences ◽  
Carboxypeptidase Y ◽  
Terminal Amino Acid ◽  
Hydrophobic Domain ◽  
Terminal Amino

Dipeptidyl peptidase IV was solubilized from the microvillar membrane of pig kidney by Triton X-100. The purified enzyme was homogeneous on polyacrylamide-gel electrophoresis and ultracentrifugation, although immunoelectrophoresis indicated that amino-peptidase M was a minor contaminant. A comparison of the detergent-solubilized and proteinase (autolysis)-solubilized forms of the enzyme was undertaken to elucidate the structure and function of the hydrophobic domain that serves to anchor the protein to the membrane. No differences in catalytic properties, nor in sensitivity to inhibition by di-isopropyl phosphorofluoridate were found. On the other hand, several structural differences could be demonstrated. Both forms were about 130,000 subunit mol.wt., but the detergent form appeared to be larger by no more than about 4,000. Electron microscopy showed both forms to be dimers, and gel filtration revealed a difference in the dimeric mol.wt. of about 38 000, mainly attributable to detergent molecules bound to the hydrophobic domain. Papain converted the detergent form into a hydrophilic form that could not be distinguished in properties from the autolysis form. A hydrophobic peptide of about 3500 mol.wt. was identified as a product of papain treatment. The detergent and proteinase forms differed in primary structure. Partial N-terminal amino acid sequences were shown to be different, and the pattern of release of amino acids from the C-terminus by carboxypeptidase Y was essentially similar. The results are consistent with a model in which the protein is anchored to the microvillar membrane by a small hydrophobic domain located within the N-terminal amino acid sequence of the polypeptide chain. The significance of these results in relation to biosynthesis of the enzyme and assembly in the membrane is discussed.

scholarly journals Carbohydrate is linked through ethanolamine to the C-terminal amino acid of Trypanosoma brucei variant surface glycoprotein

1983 ◽  
Vol 209 (1) ◽  
pp. 261-262 ◽  
Author(s):  
A A Holder
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Trypanosoma Brucei ◽  
Carboxy Group ◽  
Surface Glycoprotein ◽  
Variant Surface Glycoprotein ◽  
Side Chain ◽  
Serine Residue ◽  
Terminal Amino Acid ◽  
Terminal Amino

The C-terminal amino acid of the variant surface glycoprotein from Trypanosoma brucei is glycosylated. For two variant proteins that terminate in an aspartic acid and a serine residue respectively, it was shown that the sugar side chain is linked through ethanolamine to the alpha-carboxy group of the amino acid.

scholarly journals Crystal structure of the tripeptideN-(benzyloxycarbonyl)glycylglycyl-L-norvaline

2015 ◽  
Vol 71 (3) ◽  
pp. o216-o217
Author(s):  
Sumesh Nicholas
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bond ◽  
Amino Acid ◽  
Hydrogen Bonds ◽  
Crystal Lattice ◽  
Side Chain ◽  
Screw Axis ◽  
Terminal Amino Acid ◽  
Backbone Conformation ◽  
Terminal Amino

The title tripeptide, C17H23N3O6, contains a nonproteinogenic C-terminal amino acid residue, norvaline, which is an isomer of the amino acid valine. Norvaline, unlike valine, has an unbranched side chain. The molecule has a Gly–Gly segment which adopts an extended conformation. The norvaline residue also adopts an extended backbone conformation while its side chain has ag+tconformation. In the crystal lattice, N—H...O and O—H...O hydrogen bonds stabilize the packing. Molecules translated along the crystallographicaaxis associate through an N—H...O hydrogen bond. The remaining three hydrogen bonds are between molecules related by a21screw axis.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

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