A minimalistic cyclic ice-binding peptide from phage display

Corey A. Stevens, Fabienne Bachtiger, Xu-Dong Kong, Luciano A. Abriata, Gabriele C. Sosso, Matthew I. Gibson and Harm-Anton Klok ()
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Corey A. Stevens: Laboratoire des Polymères, Institut des Matériaux and Institut des Sciences et Ingénierie Chimiques, École Polytechnique Fédérale de Lausanne (EPFL)
Fabienne Bachtiger: University of Warwick
Xu-Dong Kong: Laboratory of Therapeutic Proteins and Peptides, Institute of Chemical Sciences and Engineering, École Polytechnique Fédérale de Lausanne (EPFL)
Luciano A. Abriata: Protein Production and Structure Core Facility and Laboratory for Biomolecular Modeling, École Polytechnique Fédérale de Lausanne (EPFL) and Swiss Institute of Bioinformatics
Gabriele C. Sosso: University of Warwick
Matthew I. Gibson: University of Warwick
Harm-Anton Klok: Laboratoire des Polymères, Institut des Matériaux and Institut des Sciences et Ingénierie Chimiques, École Polytechnique Fédérale de Lausanne (EPFL)

Nature Communications, 2021, vol. 12, issue 1, 1-8

Abstract: Abstract Developing molecules that emulate the properties of naturally occurring ice-binding proteins (IBPs) is a daunting challenge. Rather than relying on the (limited) existing structure–property relationships that have been established for IBPs, here we report the use of phage display for the identification of short peptide mimics of IBPs. To this end, an ice-affinity selection protocol is developed, which enables the selection of a cyclic ice-binding peptide containing just 14 amino acids. Mutational analysis identifies three residues, Asp8, Thr10 and Thr14, which are found to be essential for ice binding. Molecular dynamics simulations reveal that the side chain of Thr10 hydrophobically binds to ice revealing a potential mechanism. To demonstrate the biotechnological potential of this peptide, it is expressed as a fusion (‘Ice-Tag’) with mCherry and used to purify proteins directly from cell lysate.

Date: 2021
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DOI: 10.1038/s41467-021-22883-w

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