AMINO ACID DISTRIBUTION IN BIOLOGICALLY ACTIVE PEPTIDES

1960 ◽  
Vol 38 (4) ◽  
pp. 477-481 ◽  
Author(s):  
Saul B. Needleman ◽  
R. Quentin Blackwell ◽  
Leonard S. Fosdick
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Biologically Active ◽  
Amino Acid Distribution ◽  
Chi Square ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Unusual Occurrence ◽  
Specific Peptide

A group of biologically active peptides were examined for possible favored chain positions exhibited by some of the 21 constituent amino acids as well as for the unusual occurrence of specific peptide linkages. High levels of significance were revealed for certain amino acid couplets when they were subjected to chi-square analyses.

scholarly journals The application of ketimine derivatives of amino acids to peptide synthesis

1976 ◽  
Vol 29 (7) ◽  
pp. 1591 ◽  
Author(s):  
AP Hope ◽  
B Halpern
Keyword(s):  
Amino Acids ◽  
Acetic Acid ◽  
Amino Acid ◽  
Biologically Active ◽  
Amino Acid Esters ◽  
Protecting Group ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Derivatives Of ◽  
Acid Esters

N-(2-Hydroxyarylmethy1ene)amino acids have been coupled with amino acid esters to form sterically pure N-protected dipeptide esters. The protecting group can be removed by means of 80% acetic acid under conditions which leaves the t-butyloxycarbonyl protecting group intact. Biologically active peptides which are C-terminal partial sequences of substance P were prepared and were shown to have the expected vasodilator, spasmogenic and venoconstrictor properties.

New Chemical Descriptors Relevant for the Design of Biologically Active Peptides. A Multivariate Characterization of 87 Amino Acids

1998 ◽  
Vol 41 (14) ◽  
pp. 2481-2491 ◽  
Author(s):  
Maria Sandberg ◽  
Lennart Eriksson ◽  
Jörgen Jonsson ◽  
Michael Sjöström ◽  
Svante Wold
Keyword(s):  
Amino Acids ◽  
Biologically Active ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Chemical Descriptors

scholarly journals MALDI TOF/TOF-Based Approach for the Identification ofd- Amino Acids in Biologically Active Peptides and Proteins

2016 ◽  
Vol 15 (5) ◽  
pp. 1487-1496 ◽  
Author(s):  
Johannes Koehbach ◽  
Christian W. Gruber ◽  
Christian Becker ◽  
David P. Kreil ◽  
Alexander Jilek
Keyword(s):  
Amino Acids ◽  
Biologically Active ◽  
Active Peptides ◽  
Maldi Tof ◽  
Biologically Active Peptides

scholarly journals Design and synthesis of biologically active peptides: A ‘tail’ of amino acids can modulate activity of synthetic cyclic peptides

Peptides ◽  
2011 ◽  
Vol 32 (12) ◽  
pp. 2504-2510 ◽  
Author(s):  
Alberto Bryan ◽  
Leroy Joseph ◽  
James A. Bennett ◽  
Herbert I. Jacobson ◽  
Thomas T. Andersen
Keyword(s):  
Amino Acids ◽  
Cyclic Peptides ◽  
Biologically Active ◽  
Active Peptides ◽  
Design And Synthesis ◽  
Biologically Active Peptides

scholarly journals Circular dichroism of bradykinin and related peptides

1971 ◽  
Vol 121 (2) ◽  
pp. 179-184 ◽  
Author(s):  
A. H. Brady ◽  
J. W. Ryan ◽  
J. M. Stewart
Keyword(s):  
Biological Activity ◽  
Circular Dichroism ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Molecular Interactions ◽  
Biologically Active ◽  
Spectral Features ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Circular Dichroïsm

1. The circular dichroism of bradykinin and a number of its analogues and homologues was measured over the spectral range 200–300nm. All of the biologically active peptides showed maxima at 220nm and minima at 235nm. The spectra were independent of solvent and temperature. The vibronic transitions of phenylalanyl residues in the 250–280nm range showed no evidence of intra- or inter-molecular interactions. We take this as evidence that bradykinin and its biologically active analogues and homologues exist in solution as disordered chains. 2. None of the analogues with spectra unlike bradykinin possessed biological activity. However, peptides such as retro-bradykinin, des-6-serine-bradykinin, des-1-arginine-bradykinin and des-9-arginine-bradykinin produced spectra like that of bradykinin but were devoid of biological activity. Although we could not identify spectral features that were clearly correlated with biological activity, it appears unlikely that highly ordered peptides of the same amino acid composition as bradykinin would possess bradykinin-like effects.

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