Circular dichroism (CD) studies on biological activity of mast cell degranulating (MCD) peptide analogs*

2009 ◽  
Vol 44 (5) ◽  
pp. 410-413 ◽  
Author(s):  
ANGELIKI BUKU ◽  
UROOJ MIRZA ◽  
KRZYSZTOF POLEWSKI
Keyword(s):  
Mast Cell ◽  
Biological Activity ◽  
Circular Dichroism ◽  
Peptide Analogs ◽  
Cd Studies ◽  
Circular Dichroïsm ◽  
Mast Cell Degranulating

Mast cell degranulating (MCD) peptide analogs with reduced ring structure

1992 ◽  
Vol 11 (3) ◽  
pp. 275-280 ◽  
Author(s):  
A. Buku ◽  
J. Reibman ◽  
A. Pistelli ◽  
P. Blandina ◽  
D. Gazis
Keyword(s):  
Mast Cell ◽  
Ring Structure ◽  
Peptide Analogs ◽  
Reduced Ring ◽  
Mast Cell Degranulating

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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