Interaction of smooth muscle calponin with phospholipids

Natalia V. Bogatcheva, Nikolai B. Gusev

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

Analyzing the primary structure we predicted that calponin may interact with phospholipids. In order to check this suggestion we investigated the interaction of calponin with phospholipids by ultracentrifugation, light scattering, vesicles leakage and differential scanning calorimetry. In agreement with our prediction calponin interacts with acidic phospholipids and the phospholipid-binding site was located in the short (13 kDa) N-terminal chymotryptic peptide of calponin. The apparent dissociation constant of calponin-phospholipids complex was less than 0.2 μM and calmodulin competes with phospholipids for calponin binding. Although the interaction of calponin with phospholipids decreases at high ionic strength, calponin binds phospholipids even in the presence of 100-150 mM of the salt. Under certain conditions calponin induced leakage of phospholipid vesicles and affected the cooperativity of lipid phase transition. It is concluded that both electrostatic and hydrophobic interactions provide for calponin-phospholipid complex formation.

Original languageEnglish (US)
Pages (from-to)123-126
Number of pages4
JournalFEBS Letters
Volume371
Issue number2
DOIs
StatePublished - Sep 4 1995

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Keywords

  • Calmodulin
  • Calponin
  • Differential scanning calorimetry
  • Light scattering
  • Phospholipid
  • Ultracentrifugation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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