Structure‐function relationships in the polypeptide cardiac stimulant, anthopleurin‐A: Effects of limited proteolysis by trypsin

Alison R. GOULD, Bridget C. MABBUTT, Raymond S. NORTON

Research output: Contribution to journalArticleResearchpeer-review

14 Citations (Scopus)

Abstract

Selective proteolysis of the polypeptide cardiostimulant anthopleurin‐A by trypsin introduces a single break in the polypeptide backbone on the C‐terminal side of Arg14. The resulting derivative is devoid of any cardiostimulant activity. The structural changes which accompany this loss of activity have been examined by one‐ and two‐ dimensional 1H‐NMR spectroscopy. It is shown that the overall backbone folding of anthopleurin‐A is conserved on digestion, with some structural changes occurring for residues which are adjacent to the site of cleavage by trypsin. Thus, although previous NMR studies on anthopleurin‐A indicate that the region surrounding Arg14 is devoid of any ordered structure, it appears that some degree of structural integrity is required to allow the essential side chains to adopt the conformation necessary to produce a cardiostimulant effect.

Original languageEnglish
Pages (from-to)145-153
Number of pages9
JournalEuropean Journal of Biochemistry
Volume189
Issue number1
DOIs
Publication statusPublished - 1990
Externally publishedYes

Cite this

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Structure‐function relationships in the polypeptide cardiac stimulant, anthopleurin‐A : Effects of limited proteolysis by trypsin. / GOULD, Alison R.; MABBUTT, Bridget C.; NORTON, Raymond S.

In: European Journal of Biochemistry, Vol. 189, No. 1, 1990, p. 145-153.

Research output: Contribution to journalArticleResearchpeer-review

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AB - Selective proteolysis of the polypeptide cardiostimulant anthopleurin‐A by trypsin introduces a single break in the polypeptide backbone on the C‐terminal side of Arg14. The resulting derivative is devoid of any cardiostimulant activity. The structural changes which accompany this loss of activity have been examined by one‐ and two‐ dimensional 1H‐NMR spectroscopy. It is shown that the overall backbone folding of anthopleurin‐A is conserved on digestion, with some structural changes occurring for residues which are adjacent to the site of cleavage by trypsin. Thus, although previous NMR studies on anthopleurin‐A indicate that the region surrounding Arg14 is devoid of any ordered structure, it appears that some degree of structural integrity is required to allow the essential side chains to adopt the conformation necessary to produce a cardiostimulant effect.

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