Issue 13, 2020

On the microscopic origin of the cryoprotective effect in lysine solutions

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.

Graphical abstract: On the microscopic origin of the cryoprotective effect in lysine solutions

Supplementary files

Article information

Article type
Paper
Submitted
15 Nov 2019
Accepted
05 Mar 2020
First published
06 Mar 2020

Phys. Chem. Chem. Phys., 2020,22, 6919-6927

On the microscopic origin of the cryoprotective effect in lysine solutions

A. Henao, G. N. Ruiz, N. Steinke, S. Cerveny, R. Macovez, E. Guàrdia, S. Busch, S. E. McLain, C. D. Lorenz and L. C. Pardo, Phys. Chem. Chem. Phys., 2020, 22, 6919 DOI: 10.1039/C9CP06192D

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements