Ice Recrystallization Inhibition by Amino Acids: The Curious Case of Alpha- and Beta-Alanine. Warren, M. T., Galpin, I., Bachtiger, F., Gibson, M. I., & Sosso, G. C. The Journal of Physical Chemistry Letters, 13(9):2237–2244, March, 2022. Publisher: American Chemical Society![Ice Recrystallization Inhibition by Amino Acids: The Curious Case of Alpha- and Beta-Alanine [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Extremophiles produce macromolecules which inhibit ice recrystallization, but there is increasing interest in discovering and developing small molecules that can modulate ice growth. Realizing their potential requires an understanding of how these molecules function at the atomistic level. Here, we report the discovery that the amino acid l-α-alanine demonstrates ice recrystallization inhibition (IRI) activity, functioning at 100 mM (∼10 mg/mL). We combined experimental assays with molecular simulations to investigate this IRI agent, drawing comparison to β-alanine, an isomer of l-α-alanine which displays no IRI activity. We found that the difference in the IRI activity of these molecules does not originate from their ice binding affinity, but from their capacity to (not) become overgrown, dictated by the degree of structural (in)compatibility within the growing ice lattice. These findings shed new light on the microscopic mechanisms of small molecule cryoprotectants, particularly in terms of their molecular structure and overgrowth by ice.
@article{warren_ice_2022,
title = {Ice {Recrystallization} {Inhibition} by {Amino} {Acids}: {The} {Curious} {Case} of {Alpha}- and {Beta}-{Alanine}},
volume = {13},
shorttitle = {Ice {Recrystallization} {Inhibition} by {Amino} {Acids}},
url = {https://doi.org/10.1021/acs.jpclett.1c04080},
doi = {10.1021/acs.jpclett.1c04080},
abstract = {Extremophiles produce macromolecules which inhibit ice recrystallization, but there is increasing interest in discovering and developing small molecules that can modulate ice growth. Realizing their potential requires an understanding of how these molecules function at the atomistic level. Here, we report the discovery that the amino acid l-α-alanine demonstrates ice recrystallization inhibition (IRI) activity, functioning at 100 mM (∼10 mg/mL). We combined experimental assays with molecular simulations to investigate this IRI agent, drawing comparison to β-alanine, an isomer of l-α-alanine which displays no IRI activity. We found that the difference in the IRI activity of these molecules does not originate from their ice binding affinity, but from their capacity to (not) become overgrown, dictated by the degree of structural (in)compatibility within the growing ice lattice. These findings shed new light on the microscopic mechanisms of small molecule cryoprotectants, particularly in terms of their molecular structure and overgrowth by ice.},
number = {9},
urldate = {2022-05-10},
journal = {The Journal of Physical Chemistry Letters},
author = {Warren, Matthew T. and Galpin, Iain and Bachtiger, Fabienne and Gibson, Matthew I. and Sosso, Gabriele C.},
month = mar,
year = {2022},
note = {Publisher: American Chemical Society},
pages = {2237--2244},
}
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