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Elastin recoil is driven by the hydrophobic effect.

Nour M Jamhawi1, Ronald L Koder2,3, Richard J Wittebort1

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|March 5, 2024
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The hydrophobic effect, not entropic recoil, drives elastin function in vertebrates. This finding explains elastin's resilience and longevity, crucial for arteries and lungs.

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Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Elastin is a vital extracellular matrix protein in vertebrates, providing elasticity to tissues like arteries, lungs, and skin.
  • Its remarkable resilience, enduring billions of cycles without replacement, is key to tissue function and longevity.
  • The long-standing debate over elastin's recoil mechanism, whether entropic or otherwise, has persisted for over five decades.

Purpose of the Study:

  • To elucidate the primary driving force behind elastin's elastic recoil mechanism.
  • To investigate the role of water ordering and thermodynamic properties in elastin's function.
  • To challenge the prevailing entropic recoil theory and propose an alternative mechanism.

Main Methods:

  • Utilized a combined Nuclear Magnetic Resonance (NMR) and thermomechanical study.
  • Observed water ordering at the solvent:protein interface using double quantum 2H NMR as a function of stretch.
  • Conducted extensive thermodynamic analysis by measuring elastin length and volume under varying force, temperature, and solvent conditions.

Main Results:

  • Demonstrated that water ordering at the solvent:protein interface increases proportionally with elastin stretching.
  • Observed increased heat capacity and decreased internal energy upon stretching, with heat released exceeding work performed.
  • Thermodynamic signatures were altered by cosolvents that modify the hydrophobic effect, supporting its role.

Conclusions:

  • The hydrophobic effect, not configurational entropy, is the primary driver of elastin recoil under physiological conditions.
  • This mechanism explains elastin's exceptional resilience and resistance to hardening, unlike rubber.
  • The hydrophobic effect-driven recoil is proposed as the fundamental origin of elastin's unique properties and longevity.