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On the Physical Basis of Biological Signaling by Interface Pulses.

Langmuir : the ACS journal of surfaces and colloids·2018
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Specific Regulation of Enzymatic Activity by Interface Pulses.

Daniel T Hanisch1, Matthias F Schneider1

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Enzyme activity is regulated by the physical state of its interface, not molecular changes. Specific interface pulses that increase pressure and density enhance enzyme activity, while others decrease it.

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Area of Science:

  • Biophysics
  • Biochemistry
  • Physical Chemistry

Background:

  • Enzymatic activity is influenced by the thermodynamic state of the interface where the enzyme is located.
  • Previous studies showed a correlation between maximum enzyme activity and maximum compressibility.
  • Interface pulses can alter the interface state and modulate enzyme activity, as seen with acetylcholinesterase (AChE).

Purpose of the Study:

  • To investigate how different types of interface pulses specifically modulate enzyme activity.
  • To explore the role of thermodynamic parameters like pressure and density in enzyme regulation.
  • To validate a physical mechanism for enzyme-enzyme communication.

Main Methods:

  • Utilized membrane-embedded phospholipase A2 (PLA2) as a model enzyme.
  • Monitored enzyme activity by measuring lateral pressure at the interface, eliminating the need for additional assays.
  • Applied different types of interface pulses to observe their effects on enzyme activity and interface state.

Main Results:

  • Enzyme activity modulation by interface pulses is dependent on the specific type of pulse.
  • Pulses that increase interface pressure and lateral density enhance PLA2 enzymatic activity.
  • Pulses that decrease interface pressure lead to a reduction in PLA2 activity.

Conclusions:

  • Enzyme activity is regulated by physical, thermodynamic parameters of the interface, such as compressibility, lateral density, and pressure.
  • Specific interface pulse types differentially affect enzyme activity by altering these thermodynamic parameters.
  • These findings support a physical mechanism for enzyme-enzyme communication, emphasizing thermodynamic state over specific molecular modifications.