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Mechanical Activation Drastically Accelerates Amide Bond Hydrolysis, Matching Enzyme Activity.

Michael F Pill1,2, Allan L L East3, Dominik Marx4

  • 1Department of Applied Sciences and Mechatronics, Munich University of Applied Sciences, Lothstrasse 34, 80334, Munich, Germany.

Angewandte Chemie (International Ed. in English)
|May 22, 2019
PubMed
Summary

Mechanical force drastically accelerates amide hydrolysis, challenging previous beliefs about amide bond stability. This discovery has implications for macromolecular waste recycling and enzyme design.

Keywords:
ab initio calculationsmechanical propertiespeptidesproteinssingle-molecule studies

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Area of Science:

  • Biochemistry
  • Materials Science
  • Physical Chemistry

Background:

  • Amide bonds, including peptide bonds, confer strength to proteins and synthetic polyamides.
  • Proteins and polyamides withstand mechanical force, but the effect of force on amide bond stability was unknown.

Purpose of the Study:

  • To investigate the impact of mechanical force on amide and peptide bond stability.
  • To elucidate the mechanism and kinetics of force-induced amide hydrolysis.

Main Methods:

  • Single-molecule force spectroscopy (SMFS) to apply and measure picoNewton forces.
  • Quantum mechanochemical ab initio calculations to model amide hydrolysis.

Main Results:

  • Forces of a few hundred picoNewtons (pN) accelerate amide hydrolysis by a factor of 10^9.
  • Low-force acceleration is followed by moderate acceleration at nanoNewton (nN) forces.
  • Experimental findings are explained by quantum mechanochemical calculations.

Conclusions:

  • Amide bond stability is significantly dependent on applied mechanical force.
  • Mechanical activation plays a crucial role in amide hydrolysis.
  • Findings suggest applications in macromolecular waste recycling and bioengineered enzyme design.