On the microscopic origin of the cryoprotective effect in lysine solutions

Andrés Henao, Guadalupe N Ruiz, Nicola Steinke, Silvina Cerveny, Roberto Macovez, Elvira Guàrdia, Sebastian Busch, Sylvia E McLain, Christian D Lorenz, Luis Carlos Pardo

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


The amino acid lysine has been shown to prevent water crystallization at low temperatures in saturated aqueous solutions [S. Cerveny and J. Swenson, Phys. Chem. Chem. Phys., 2014, 16, 22382-22390]. Here, we investigate two ratios of water and lysine (5.4 water molecules per lysine (saturated) and 11 water molecules per lysine) by means of the complementary use of computer simulations and neutron diffraction. By performing a detailed structural analysis we have been able to explain the anti-freeze properties of lysine by the strong hydrogen bond interactions of interstitial water molecules with lysine that prevent them from forming crystalline seeds. Additional water molecules beyond the 1 : 5.4 proportion are no longer tightly bonded to lysine and therefore are free to form crystals.

Original languageEnglish
Pages (from-to)6919-6927
Number of pages9
JournalPhysical Chemistry Chemical Physics
Issue number13
Publication statusPublished - 7 Apr 2020


  • Computer Simulation
  • Cryoprotective Agents/chemistry
  • Crystallization
  • Hydrogen Bonding
  • Lysine/chemistry
  • Models, Molecular
  • Neutron Diffraction
  • Solutions/chemistry
  • Water/chemistry


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