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

18 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)
Pages (from-to)	7658-7661
Number of pages	4
Journal	Chemical Communications
Volume	58
Issue number	55
DOIs	https://doi.org/10.1039/d2cc02531k
State	Published - Jul 14 2022

All Science Journal Classification (ASJC) codes

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

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10.1039/d2cc02531k

Cite this

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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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doi = "10.1039/d2cc02531k",

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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 - 2022/7/14

Y1 - 2022/7/14

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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UR - https://www.scopus.com/pages/publications/85132868938#tab=citedBy

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DO - 10.1039/d2cc02531k

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AN - SCOPUS:85132868938

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VL - 58

SP - 7658

EP - 7661

JO - Chemical Communications

JF - Chemical Communications

IS - 55

ER -

Minimalistic ice recrystallisation inhibitors based on phenylalanine

Abstract

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