Cold-adapted organisms produce antifreeze proteins and glycoproteins to control the growth, melting and recrystallization of ice. It has been proposed that these molecules pin the crystal surface, creating a curvature that arrests the growth and melting of the crystal. Here we use thermodynamic modeling and molecular simulations to demonstrate that the curvature of the superheated or supercooled surface depends on the temperature and distances between ice-binding molecules, but not the details of their interactions with ice. We perform simulations of ice pinned with the antifreeze protein TmAFP, polyvinyl alcohol with different degrees of polymerization, and model ice-binding molecules to determine the thermal hystereses on melting and freezing, i.e. the maximum curvature that can be attained before, respectively, ice melts or grows irreversibly over the ice-binding molecules. We find that the thermal hysteresis is controlled by the bulkiness of the ice-binding molecules and their footprint at the ice surface. We elucidate the origin of the asymmetry between freezing and melting hysteresis found in experiments and propose guidelines to design synthetic antifreeze molecules with potent thermal hysteresis activity.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1021/acs.jpclett.8b00300 | DOI Listing |
J Chem Phys
October 2024
Faculty of Chemistry, Department of Physical Chemistry, Gdańsk University of Technology, Narutowicza 11/12, 80-233 Gdańsk, Poland.
In 2012, the molecular structure of a new, broad class of ice-binding proteins, classified as "domain of unknown function" (DUF) 3494, was described for the first time. These proteins have a common tertiary structure and are characterized by a very wide spectrum of antifreeze activity (from weakly active to hyperactive). The ice-binding surface (IBS) region of these molecules differs significantly in its structure from the IBS of previously known antifreeze proteins (AFPs), showing a complete lack of regularity and high hydrophilicity.
View Article and Find Full Text PDFInt J Biol Macromol
October 2024
National Key Laboratory of Science and Technology on Advanced Composites in Special Environments, Center for Composite Materials and Structures, Harbin Institute of Technology, Harbin 150080, China; Shenzhen STRONG Advanced Materials Research Institute Co. Ltd., Shenzhen 518035, China. Electronic address:
Antifreeze proteins (AFPs) can inhibit ice crystal growth. The ice-binding mechanism of AFPs remains unclear, yet the hydration shells of AFPs are thought to play an important role in modulating the binding of AFPs and ice. Here, we performed all-atom molecular dynamics simulations of an AFP from Choristoneura fumiferana (CfAFP) at four different temperatures, with a focus on analysis at 240 and 300 K, to investigate the dynamic and thermodynamic characteristics of hydration shells around ice-binding surfaces (IBS) and non-ice-binding surfaces (NIBS).
View Article and Find Full Text PDFInt J Biol Macromol
August 2024
Faculty of Biological Science, Akwa-Ibom State University, Akwa-Ibom State, Uyo 1167, Nigeria; College of Food Science and Engineering, Central South University of Forestry and Technology, 498 South Shaoshan Road, Changsha 410004, China. Electronic address:
Microorganisms' ice-binding structures (IBS) are macromolecules with potential commercial value in agriculture, food technology, material technology, cryobiology, and medicine. Microbial ice-structuring or microbial ice-binding particles, with their multi-applications, are simple to use, effective in low amounts, non-toxic, and environmentally friendly. Due to their source and composition diversities, microbial ice-binding structures are gaining attention because they are useable in various conditions.
View Article and Find Full Text PDFInt J Biol Macromol
May 2024
College of Food Science and Technology, Zhejiang University of Technology, Hangzhou, China; Zhejiang Key Laboratory of Green, Low-carbon and Efficient Development of Marine Fishery Resources, Hangzhou 310014, China; National R&D Branch Center for Pelagic Aquatic Products Processing (Hangzhou), Hangzhou, China; Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, China. Electronic address:
Cryo Letters
April 2024
Department of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, ON, Canada.
Despite the routine use of cryopreservation for the storage of biological materials, its outcomes are often sub-optimal (including reduced post-thaw viability, recovery, and functionality) due to the damage caused by uncontrolled ice growth. Traditional cryoprotective agents (CPAs), including dimethyl sulfoxide (DMSO), fail to prevent damage caused by ice growth and concerns over CPA cytotoxicity have fostered an increased interest in developing improved CPAs and cryoprotection strategies. The inhibition of ice recrystallization by natural antifreeze (glyco)proteins [AF(G)Ps] to improve cryopreservation outcomes has been examined; however, the ice binding properties of these substances and their challenging large-scale production make them poor CPA candidates.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!