[Studies on the mechanism of action of peptides attacking smooth muscles. III. The effect of N-azylation on the activity of C-terminal partial sequences of eledoisin, physalaemin and substance P on the guinea pig ileum].

Paper

[Studies on the mechanism of action of peptides attacking smooth muscles. III. The effect of N-azylation on the activity of C-terminal partial sequences of eledoisin, physalaemin and substance P on the guinea pig ileum].

Published 1975 · H. Niedrich, M. Bienert, B. Mehlis

Acta biologica et medica Germanica

UNKNOWN SJR score

1

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0

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Semantic Scholar

Abstract

C-terminal pentapeptides of eledoisin, physalaemin, and the substance P, when N-substituted with acetyl, halogenacetyl and other acyl residues, are increased in their action more than 100fold, reaching the activity of acylated hexa- and heptapeptides. The effect found with a number of compounds is interpreted as the influence of predominantly hydrophobic substituents upon the peptide sequence essential for the action. Polar groups in the acylic residue seem to cause additional increase in action.

In Vitro Study

Study Snapshot

N-azylation of C-terminal pentapeptides of eledoisin, physalaemin, and substance P increases their activity more than 100fold, mainly due to hydrophobic substituents and polar groups in the acylic residue.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Paper

[Studies on the mechanism of action of peptides attacking smooth muscles. III. The effect of N-azylation on the activity of C-terminal partial sequences of eledoisin, physalaemin and substance P on the guinea pig ileum].

References

Citations

Antidiuretic activities of substance P and its analogs

Substance P and its analogs with C-terminal hexapeptides show potent antidiuretic activity, while weaker analogs show weaker activity, and acylation increases activity.