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Intrinsic selectivity in binding of matrix metalloproteinase-7 to differently charged lipid membranes

Bratati Ganguly1, Jayati Banerjee, Adekunle I Elegbede

  • 1Department of Chemistry, Biochemistry and Molecular Biology, North Dakota State University, Fargo, ND 58105, USA.

FEBS Letters
|November 27, 2007
PubMed

Insights

Matrix metalloproteinase-7 (MMP-7) binds to lipid membranes, with strongest interaction occurring with anionic membranes. Enzyme activity is impaired by positively charged membranes due to electrostatic surface potentials.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Matrix metalloproteinase-7 (MMP-7) is a key enzyme involved in tissue remodeling and disease.
  • Understanding MMP-7's interaction with biological membranes is crucial for elucidating its function and regulation.
  • Lipid membranes play a significant role in modulating protein activity and localization.

Purpose of the Study:

  • To investigate the interaction of MMP-7 with different types of lipid membranes (anionic, cationic, neutral).
  • To determine how membrane charge affects the catalytic activity of MMP-7.
  • To elucidate the structural basis for MMP-7's differential membrane interactions.

Main Methods:

  • Liposome binding assays to assess MMP-7 interaction with various lipid compositions.
  • Enzyme activity assays to measure catalytic function upon membrane binding.
  • Analysis of crystallographic structures to examine surface electrostatic potentials.

Main Results:

  • MMP-7 exhibits varying degrees of interaction with anionic, cationic, and neutral lipid membranes, with the strongest affinity for anionic membranes.
  • Catalytic activity of MMP-7 is preserved upon binding to neutral and anionic membranes.
  • Binding to cationic membranes significantly impairs MMP-7's catalytic activity.
  • Structural analysis reveals a bipolar distribution of electrostatic surface potentials on MMP-7, explaining its charge-dependent interactions.

Conclusions:

  • MMP-7's interaction with lipid membranes is strongly influenced by membrane charge.
  • The enzyme's catalytic activity is modulated by electrostatic interactions with the membrane surface.
  • The bipolar electrostatic surface potential of MMP-7 is a key determinant of its membrane binding and activity modulation.

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