A peptide mimetic of calcium

Academic Article


  • Proteins of the troponin superfamily use homologous amino acid sequences as binding sites for Ca2+ and seem to have evolved from an ancestral Ca2+ binding site. We have utilized this ancestral sequence to construct a peptide (Ca2+-like peptide) with inverted hydropathy to the calcium-coordinating region of this protein. This synthetic peptide acted like Ca2+ in that (i) it increased the calmodulin-dependent hydrolysis of cAMP by phosphodiesterase, (ii) it interacted with EDTA, and (iii) it enhanced contraction of urinary bladder smooth muscle in vitro. Unlike Ca2+, the peptide's effects were destroyed by acid hydrolysis. These findings demonstrate the synthesis of a peptide that can substitute for Ca2+ and may have considerable utility for the study of Ca2+-regulated pathways and possible therapeutic value as a pharmacologic agent.
  • Digital Object Identifier (doi)

    Pubmed Id

  • 1714451
  • Author List

  • Dillon J; Thomas Woods W; Guarcello V; Leboeuf RD; Blalock JE
  • Start Page

  • 9726
  • End Page

  • 9729
  • Volume

  • 88
  • Issue

  • 21