On the microscopic origin of the cryoprotective effect in lysine solutions.

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ID: 105405
2020
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Ranked #61 of 184 articles by views in Physical chemistry chemical physics : PCCP

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Abstract
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.
Reference Key
henao2020onphysical Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Henao, Andrés;Ruiz, Guadalupe N;Steinke, Nicola;Cerveny, Silvina;Macovez, Roberto;Guàrdia, Elvira;Busch, Sebastian;McLain, Sylvia E;Lorenz, Christian D;Pardo, Luis Carlos;
Journal Physical chemistry chemical physics : PCCP
Year 2020
DOI
10.1039/c9cp06192d
URL
Keywords
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