Antifreeze glycoprotein agents: structural requirements for activity

Abstract

Antifreeze glycoproteins (AFGPs) are considered to be the most efficient means to reduce ice damage to cell tissues since they are able to inhibit growth and crystallization of ice. The key element of antifreeze proteins is to act in a non-colligative manner which allows them to function at concentrations 300-500 times lowers than other dissolved solutes. During the past decade, AFGPs have demonstrated tremendous potential for many pharmaceutical and food applications. Presently, the only route to obtain AFGPs involves the time consuming and expensive process of isolation and purification from deep-sea polar fishes. Unfortunately, it is not amenable to mass production and commercial applications. The lack of understanding of the mechanism through which the AFGPs inhibit ice growth has also hampered the realization of industrial and biotechnological applications. Here we report the structural motifs that are essential for antifreeze activity of AFGPs, and propose a unified mechanism based on both recent studies of short alanine peptides and structure activity relationship of synthesized AFGPs.

Design and activity of novel lactoferrampin analogues against O157:H7 enterohemorrhagic escherichia coli

“…Each spectrum was obtained as an average of three scans taken at a rate of 20 (nm/min) with a spectral band of 1nm. Each experiment was repeated four times and averages were taken of the resulting data …”

Molecular Dynamics Simulation for Mechanism Elucidation of Food Processing and Safety: State of the Art

“…The interaction between antifreeze proteins (AFPs) and water has intrigued many researchers, particularly to elucidate the mechanisms whereby the AFP inhibits the formation of ice crystals (Carvajal-Rondanelli, Marshall, & Guzman, 2011;Matsumoto, Saito, & Ohmine, 2002;Petzold & Aguilera, 2009). MD simulations on AFP indicated that the solvation water around the protein molecule preconfigured the ice-binding face.…”

Antivirulence Properties of an Antifreeze Protein

“…Additional properties of AFPs include the inhibition of ice recrystallization or cell membrane stabilization at low temperatures (Davies and Sykes, 1997, Venketesh and Dayananda, 2008). Antifreeze glycoproteins (AFGPs), a class of AFPs, are characterized by canonical Ala-Ala-Thr or Pro-Ala-Thr repeats with a β-D-galactosyl-(1→3)-α-N-acetyl-D-galactosamine disaccharide attached to each threonine (Carvajal-Rondanelli et al, 2011). Arctic fish AFGPs contain between 4 to 55 repeats, and AFGPs of different length may synergize, suggesting functional differences encoded into the number of tripeptide repeats and spacer sequences between them (Garner and Harding, 2010).…”