Minimalistic ice recrystallisation inhibitors based on phenylalanine

Matthew T. Warren; Iain Galpin; Muhammad Hasan; Steven A. Hindmarsh; John D. Padrnos; Charlotte Edwards-Gayle; Robert T. Mathers; Dave J. Adams; Gabriele C. Sosso; Matthew I. Gibson

doi:10.1039/d2cc02531k

Minimalistic ice recrystallisation inhibitors based on phenylalanine

Matthew T. Warren, Iain Galpin, Muhammad Hasan, Steven A. Hindmarsh, John D. Padrnos, Charlotte Edwards-Gayle, Robert T. Mathers, Dave J. Adams, Gabriele C. Sosso, Matthew I. Gibson

Penn State New Kensington

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

Ice recrystallisation inhibition (IRI) is typically associated with ice binding proteins, but polymers and other mimetics are emerging. Here we identify phenylalanine as a minimalistic, yet potent, small-molecule IRI capable of inhibiting ice growth at just 1 mg mL⁻¹. Facial amphiphilicity is shown to be a crucial structural feature, with para-substituents enhancing (hydrophobic) or decreasing (hydrophilic) IRI activity. Both amino and acid groups were found to be essential. Solution-phase self-assembly of Phenylalanine was not observed, but the role of self-assembly at the ice/water interface could not be ruled out as a contributing factor.

Original language	English (US)
Journal	Chemical Communications
DOIs	https://doi.org/10.1039/d2cc02531k
State	Accepted/In press - 2022

All Science Journal Classification (ASJC) codes

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/d2cc02531k

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title = "Minimalistic ice recrystallisation inhibitors based on phenylalanine",

abstract = "Ice recrystallisation inhibition (IRI) is typically associated with ice binding proteins, but polymers and other mimetics are emerging. Here we identify phenylalanine as a minimalistic, yet potent, small-molecule IRI capable of inhibiting ice growth at just 1 mg mL−1. Facial amphiphilicity is shown to be a crucial structural feature, with para-substituents enhancing (hydrophobic) or decreasing (hydrophilic) IRI activity. Both amino and acid groups were found to be essential. Solution-phase self-assembly of Phenylalanine was not observed, but the role of self-assembly at the ice/water interface could not be ruled out as a contributing factor.",

author = "Warren, {Matthew T.} and Iain Galpin and Muhammad Hasan and Hindmarsh, {Steven A.} and Padrnos, {John D.} and Charlotte Edwards-Gayle and Mathers, {Robert T.} and Adams, {Dave J.} and Sosso, {Gabriele C.} and Gibson, {Matthew I.}",

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year = "2022",

doi = "10.1039/d2cc02531k",

language = "English (US)",

journal = "Chemical Communications",

issn = "1359-7345",

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TY - JOUR

T1 - Minimalistic ice recrystallisation inhibitors based on phenylalanine

AU - Warren, Matthew T.

AU - Galpin, Iain

AU - Hasan, Muhammad

AU - Hindmarsh, Steven A.

AU - Padrnos, John D.

AU - Edwards-Gayle, Charlotte

AU - Mathers, Robert T.

AU - Adams, Dave J.

AU - Sosso, Gabriele C.

AU - Gibson, Matthew I.

PY - 2022

Y1 - 2022

N2 - Ice recrystallisation inhibition (IRI) is typically associated with ice binding proteins, but polymers and other mimetics are emerging. Here we identify phenylalanine as a minimalistic, yet potent, small-molecule IRI capable of inhibiting ice growth at just 1 mg mL−1. Facial amphiphilicity is shown to be a crucial structural feature, with para-substituents enhancing (hydrophobic) or decreasing (hydrophilic) IRI activity. Both amino and acid groups were found to be essential. Solution-phase self-assembly of Phenylalanine was not observed, but the role of self-assembly at the ice/water interface could not be ruled out as a contributing factor.

AB - Ice recrystallisation inhibition (IRI) is typically associated with ice binding proteins, but polymers and other mimetics are emerging. Here we identify phenylalanine as a minimalistic, yet potent, small-molecule IRI capable of inhibiting ice growth at just 1 mg mL−1. Facial amphiphilicity is shown to be a crucial structural feature, with para-substituents enhancing (hydrophobic) or decreasing (hydrophilic) IRI activity. Both amino and acid groups were found to be essential. Solution-phase self-assembly of Phenylalanine was not observed, but the role of self-assembly at the ice/water interface could not be ruled out as a contributing factor.

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SN - 1359-7345

JO - Chemical Communications

JF - Chemical Communications

ER -

Minimalistic ice recrystallisation inhibitors based on phenylalanine

Abstract

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