Antifreeze (Glyco)protein Mimetic Behavior of Poly(vinyl alcohol): Detailed Structure Ice Recrystallization Inhibition Activity Study

• Published in: Biomacromolecules Vol. 14; no. 5; pp. 1578 - 1586
• Main Authors: Congdon, Thomas, Notman, Rebecca, Gibson, Matthew I
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 13.05.2013
• Subjects: Antifreeze Proteins - chemistry; Applied sciences; Biomimetic Materials - chemistry; Cryoprotective Agents - chemistry; Crystallization; Exact sciences and technology; Glycoproteins - chemistry; Hydrophobic and Hydrophilic Interactions; Ice; Molecular Conformation; Molecular Weight; Organic polymers; Physicochemistry of polymers; Polymerization; Polyvinyl Alcohol - chemistry; Properties and characterization; Quantitative Structure-Activity Relationship; Solution and gel properties; Property composition relationship; Vinyl alcohol copolymer; Ice; Experimental study; Polyvinylalcohol; Monodispersed polymer; Vinyl acetate copolymer; Biomimetic compound; Recrystallization; Pyrrolidone(vinyl) copolymer; Crystal growth from solutions; Aqueous solution; Mechanism of action; Antifreeze protein
• ISSN: 1525-7797; 1526-4602
• DOI: 10.1021/bm400217j

This manuscript reports a detailed study on the ability of poly(vinyl alcohol) to act as a biomimetic surrogate for antifreeze(glyco)proteins, with a focus on the specific property of ice-recrystallization inhibition (IRI). Despite over 40 years of study, the underlying mechanisms that govern the action of biological antifreezes are still poorly understood, which is in part due to their limited availability and challenging synthesis. Poly(vinyl alcohol) (PVA) has been shown to display remarkable ice recrystallization inhibition activity despite its major structural differences to native antifreeze proteins. Here, controlled radical polymerization is used to synthesize well-defined PVA, which has enabled us to obtain the first quantitative structure–activity relationships, to probe the role of molecular weight and comonomers on IRI activity. Crucially, it was found that IRI activity is “switched on” when the polymer chain length increases from 10 and 20 repeat units. Substitution of the polymer side chains with hydrophilic or hydrophobic units was found to diminish activity. Hydrophobic modifications to the backbone were slightly more tolerated than side chain modifications, which implies an unbroken sequence of hydroxyl units is necessary for activity. These results highlight that, although hydrophobic domains are key components of IRI activity, the random inclusion of addition hydrophobic units does not guarantee an increase in activity and that the actual polymer conformation is important.