1,3-Amino alcohols from 4-amino-1-aza dienes. Diastereo- and enantioselective approach to the four diastereoisomers of the N-terminal amino acid component of nikkomycins B and BX

1993 ◽  
Vol 58 (22) ◽  
pp. 5972-5975 ◽  
Author(s):  
Jose Barluenga ◽  
Argimiro L. Viado ◽  
Enrique Aguilar ◽  
Santos Fustero ◽  
Bernardo Olano
Keyword(s):  
Amino Acid ◽  
Amino Alcohols ◽  
Terminal Amino Acid ◽  
Acid Component ◽  
Amino Acid Component ◽  
Terminal Amino

Synthesis of the Four Diastereoisomers of the N-Terminal Amino Acids of Nikkomycins via Aminoalkylation with Preformed Ternary Iminium Salts

2004 ◽  
Vol 59 (4) ◽  
pp. 414-423 ◽  
Author(s):  
Jeanne Delbos-Krampe ◽  
Nikolaus Risch ◽  
Ulrich Flörke
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Silica Gel ◽  
Second Step ◽  
Terminal Amino Acid ◽  
Acid Component ◽  
Iminium Salts ◽  
Amino Acid Component ◽  
Terminal Amino

AbstractAn efficient and convenient two step synthesis of each of the four possible diastereoisomers of the N-terminal amino acid component of nikkomycins is described. We first synthesized α-amino-β-oxo acids by aminoalkylation of ketones with iminium salts. The second step using Pearlman’s catalyst gave directly nonnatural and natural precursors 13 - 16 of nikkomycins 1 which were easily separated by chromatography on silica gel.

scholarly journals Binaphthyl-anchored antibacterial tripeptide derivatives with hydrophobic C-terminal amino acid variations

2012 ◽  
Vol 8 ◽  
pp. 1265-1270 ◽  
Author(s):  
John B Bremner ◽  
Paul A Keller ◽  
Stephen G Pyne ◽  
Mark J Robertson ◽  
K Sakthivel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Staphylococcus Epidermidis ◽  
Benzyl Ester ◽  
Terminal Amino Acid ◽  
Antibiotic Resistant ◽  
Gram Positive Bacteria ◽  
Amino Acid Component ◽  
Resistant Strains ◽  
Terminal Amino

The facile synthesis of seven new dicationic tripeptide benzyl ester derivatives, with hydrophobic group variations in the C-terminal amino acid component, is described. Moderate to good activity was seen against Gram-positive bacteria in vitro. One cyclohexyl-substituted compound 2c was tested more widely and showed good potency (MIC values ranging from 2–4 μg/mL) against antibiotic-resistant strains of Staphylococcus aureus and Enterococci (VRE, VSE), and against Staphylococcus epidermidis.

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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