Calmodulin and troponin C: A comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]

Paul J. Cachia, Jennifer Van Eyk, Richard H. Ingraham, William D. McCubbin, Cyril M. Kay, Robert S. Hodges

Research output: Contribution to journalArticle

Abstract

Recent studies using bee and wasp venom peptides have led to the hypothesis that proper complex formation with calmodulin (CaM) requires the presence of a basic amphiphilic helix on the surface of the target protein [Cox, J. A. (1984) Fed. Proc., Fed. Am. Soc. Exp. Biol. 43, 3000]. We have tested this hypothesis by examining CaM and troponin C (TnC) complex formation with two basic peptides, the wasp venom tetradecapeptide mastoparan and the physiologically relevant synthetic troponin I (TnI) inhibitory peptide [104-115], using far-ultraviolet circular dichroism as a secondary structure probe. Complex formation between mastoparan and either CaM or TnC results in an increase in helical content, whereas the helical content of TnI inhibitory peptide does not increase when bound to either protein. Significantly, mastoparan is 78% α-helical in a 50% solution of the helix-inducing solvent trifluoroethanol and has a high helix-forming potential according to the Chou-Fasman rules while TnI inhibitory peptide contains none and is not predicted to have any. We interpret these data as indicating that these peptides exhibit substantially different secondary structures upon binding to CaM or TnC. The ability of mastoparan to regulate the acto-subfragment 1-tropomyosin ATPase has also been examined. Mastoparan and TnI inhibitory peptide inhibited 31% and 45% of the activity, respectively. TnC and CaM promote differing degrees of Ca2+-sensitive release of inhibition by both peptides. Sequence comparison suggests that the basic residues present in both peptides are important for binding. However, we conclude that an α-helical structure is not a prerequisite for the binding of target proteins to CaM and TnC.

Original languageEnglish (US)
Pages (from-to)3553-3562
Number of pages10
JournalBiochemistry®
Volume25
Issue number12
StatePublished - 1986
Externally publishedYes

Fingerprint

Troponin C
Troponin I
Calmodulin
Peptides
Wasp Venoms
pioglitazone
Trifluoroethanol
Bee Venoms
mastoparan
Tropomyosin
Proteins
Troponin
Circular Dichroism
Adenosine Triphosphatases
Carrier Proteins
Membrane Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Cachia, P. J., Van Eyk, J., Ingraham, R. H., McCubbin, W. D., Kay, C. M., & Hodges, R. S. (1986). Calmodulin and troponin C: A comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]. Biochemistry®, 25(12), 3553-3562.

Calmodulin and troponin C : A comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]. / Cachia, Paul J.; Van Eyk, Jennifer; Ingraham, Richard H.; McCubbin, William D.; Kay, Cyril M.; Hodges, Robert S.

In: Biochemistry®, Vol. 25, No. 12, 1986, p. 3553-3562.

Research output: Contribution to journalArticle

Cachia, PJ, Van Eyk, J, Ingraham, RH, McCubbin, WD, Kay, CM & Hodges, RS 1986, 'Calmodulin and troponin C: A comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]', Biochemistry®, vol. 25, no. 12, pp. 3553-3562.
Cachia PJ, Van Eyk J, Ingraham RH, McCubbin WD, Kay CM, Hodges RS. Calmodulin and troponin C: A comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]. Biochemistry®. 1986;25(12):3553-3562.
Cachia, Paul J. ; Van Eyk, Jennifer ; Ingraham, Richard H. ; McCubbin, William D. ; Kay, Cyril M. ; Hodges, Robert S. / Calmodulin and troponin C : A comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]. In: Biochemistry®. 1986 ; Vol. 25, No. 12. pp. 3553-3562.
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