The design of congener breaking sets to determine the function of amino acid residues in biologically active peptides

2005 ◽  
pp. 253-254
Author(s):  
James A. Burton ◽  
Timothy B. Frigo ◽  
Bore G. Raju
Keyword(s):  
Amino Acid ◽  
Biologically Active ◽  
Amino Acid Residues ◽  
Active Peptides ◽  
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.

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.

Proteases and posttranslational processing of prohormones: a review

1983 ◽  
Vol 61 (7) ◽  
pp. 501-515 ◽  
Author(s):  
Claude Lazure ◽  
Nabil G. Seidah ◽  
Didier Pélaprat ◽  
Michel Chrétien
Keyword(s):  
Amino Acid ◽  
Current Knowledge ◽  
Secretory Granules ◽  
Basic Amino Acid ◽  
Biologically Active ◽  
Maturation Process ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Precursor Molecules

Pioneering work on insulin and on lipotropin, published in 1967, led to the formulation of the hypothesis that biologically active peptides such as peptide hormones are derived from larger precursor molecules by enzymatic cleavage at basic amino acid pairs. Since then, an ever-increasing number of hormones and active peptides including neuropeptides have been found to be contained within the sequence of a larger precursor protein and are released by limited proteolytic cleavage. The hypothesis concerning the posttranslational maturation of precursor molecules into smaller active entities is now firmly established in many tissues (e.g., pituitary gland, pancreas) and for all kinds of organisms (e.g. mammals, fish), though the nature of the enzyme(s) responsible for this maturation process still remains unknown. This article presents current knowledge of the intracellular processing of precursor molecules, especially the conversion of prohormone to hormone. The discussion deals principally with the evidences concerning the localization of the maturation process mainly in the secretory granules, the role of basic amino acid pairs at the cleavage site, and the possible involvement of serine and (or) thiol endopeptidases in that process.

scholarly journals Biologically active peptides of meat and meat product proteins: a review. Part 2. Functionality of meat bioactive peptides

2020 ◽  
Vol 5 (2) ◽  
pp. 12-19
Author(s):  
I. M. Chernukha ◽  
N. G. Mashentseva ◽  
D. A. Afanasev ◽  
N. L. Vostrikova
Keyword(s):  
Amino Acid ◽  
Bioactive Peptides ◽  
Food Additives ◽  
Meat Product ◽  
Biologically Active ◽  
Food Ingredients ◽  
Active Peptides ◽  
Anticancer Properties ◽  
C Terminus ◽  
Biologically Active Peptides

Biologically active peptides (BAP) are regarded as the main products of protein hydrolysis. BAP activity depends on the amino acid sequence molecular weight and chain length, type and charge of an amino acid at the N-terminus and C-terminus, hydrophobic and hydrophilic properties, spatial structure. They positively influence many systems of the human body, including the blood circulatory, nervous, immune, gastrointestinal and other systems. The health-improving effect of bioactive peptides is formed due to their antioxidant, antihypertensive, antithrombotic, immunomodulatory, antimicrobial, anti-allergic, opioid, anti-inflammatory, hypocholesterolemic and anticancer properties. Angiotensin-I-converting enzyme (ACE) inhibitory peptides are most studied due to their effect on blood pressure regulation. Unlike synthetic preparations, biologically active peptides do not have side effects and, therefore, can be used as their alternative. There is a growing commercial interest in peptides generated from meat proteins is in the context of health saving functional foods. The paper describes prospects, pros and cons of using bioactive peptides as functional food ingredients and biologically active food additives.

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.

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