Judge, Nicola, Georgiou, Panagiotis G., Bissoyi, Akalabya, Ahmad, Ashfaq, Heise, Andreas and Gibson, Matthew I. (2023) High molecular weight polyproline as a potential biosourced ice growth inhibitor : synthesis, ice recrystallization inhibition, and specific ice face binding. Biomacromolecules, 24 (6). pp. 2459-2468. doi:10.1021/acs.biomac.2c01487 ISSN 1525-7797.

Preview

PDF WRAP-High-molecular-weight-polyproline-potential-biosourced-ice-growth-face-binding-23.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (8Mb) | Preview

Request Changes to record.

Abstract

Ice-binding proteins (IBPs) from extremophile organisms can modulate ice formation and growth. There are many (bio)technological applications of IBPs, from cryopreservation to mitigating freeze–thaw damage in concrete to frozen food texture modifiers. Extraction or expression of IBPs can be challenging to scale up, and hence polymeric biomimetics have emerged. It is, however, desirable to use biosourced monomers and heteroatom-containing backbones in polymers for in vivo or environmental applications to allow degradation. Here we investigate high molecular weight polyproline as an ice recrystallization inhibitor (IRI). Low molecular weight polyproline is known to be a weak IRI. Its activity is hypothesized to be due to the unique PPI helix it adopts, but it has not been thoroughly investigated. Here an open-to-air aqueous N-carboxyanhydride polymerization is employed to obtain polyproline with molecular weights of up to 50000 g mol–1. These polymers were found to have IRI activity down to 5 mg mL–1, unlike a control peptide of polysarcosine, which did not inhibit all ice growth at up to 40 mg mL–1. The polyprolines exhibited lower critical solution temperature behavior and assembly/aggregation observed at room temperature, which may contribute to its activity. Single ice crystal assays with polyproline led to faceting, consistent with specific ice-face binding. This work shows that non-vinyl-based polymers can be designed to inhibit ice recrystallization and may offer a more sustainable or environmentally acceptable, while synthetically scalable, route to large-scale applications.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QP Physiology R Medicine > R Medicine (General)
Divisions:	Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH):	Protein binding, Polymers in medicine, Macromolecules, Glycoproteins , Polymerization , Antifreeze proteins, Ice crystals -- Growth
Journal or Publication Title:	Biomacromolecules
Publisher:	American Chemical Society
ISSN:	1525-7797
Official Date:	12 June 2023
Dates:	Date Event 12 June 2023 Published 21 February 2023 Available 13 February 2023 Accepted
Volume:	24
Number:	6
Page Range:	pp. 2459-2468
DOI:	10.1021/acs.biomac.2c01487
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Open Access (Creative Commons)
Copyright Holders:	© 2023 The Authors. Published by American Chemical Society
Date of first compliant deposit:	22 February 2023
Date of first compliant Open Access:	22 February 2023
RIOXX Funder/Project Grant:	Project/Grant ID RIOXX Funder Name Funder ID 866056 [ERC] Horizon 2020 Framework Programme http://dx.doi.org/10.13039/100010661 899872 [ERC] Horizon 2020 Framework Programme http://dx.doi.org/10.13039/100010661 814236 [ERC] Horizon 2020 Framework Programme http://dx.doi.org/10.13039/100010661

Request changes or add full text files to a record

Repository staff actions (login required)

View Item

Downloads