Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology

Abstract

Antifreeze proteins (AFPs) and glycoproteins (AFGPs), collectively called AF(G)Ps, constitute a diverse class of proteins found in various Arctic and Antarctic fish, as well as in amphibians, plants, and insects. These compounds possess the ability to inhibit the formation of ice and are therefore essential to the survival of many marine teleost fishes that routinely encounter sub-zero temperatures. Owing to this property, AF(G)Ps have potential applications in many areas such as storage of cells or tissues at low temperature, ice slurries for refrigeration systems, and food storage. In contrast to AFGPs, which are composed of repeated tripeptide units (Ala-Ala-Thr)n with minor sequence variations, AFPs possess very different primary, secondary, and tertiary structures. The isolation and purification of AFGPs is laborious, costly, and often results in mixtures, making characterization difficult. Recent structural investigations into the mechanism by which linear and cyclic AFGPs inhibit ice crystallization have led to significant progress toward the synthesis and assessment of several synthetic mimics of AFGPs. This review article will summarize synthetic AFGP mimics as well as current challenges in designing compounds capable of mimicking AFGPs. It will also cover our recent efforts in exploring whether peptoid mimics can serve as structural and functional mimics of native AFGPs.

Physiological adaptations of yeasts living in cold environments and their potential applications

“…This kind of proteins have important functions in organisms that must tolerate freezing temperatures, as they lower the freezing point of a solution without affecting its melting point (thermal hysteresis, TH) and inhibits ice crystallization (Davies et al 2002;Bang et al 2013). In microorganisms that inhabit environments covered with ice, the secretion of IBPs probably helps in retention of a liquid environment surrounding the cells and maintains water channels necessary for nutrients fluxes, while still allowing the attachment of the microorganism to ice (i.e., to form biofilms) (Davies 2014).…”

Sequencing and Expression Characterization of Antifreeze Protein Maxi-Like in Apis cerana cerana

“…These small compounds primarily consist of hydrocarbons, amino acids, and polyols, which are involved in energy metabolism and accumulation of cryoprotectants ( Holden and Storey 1994 ). The antifreeze proteins (AFPs), antifreeze glycoproteins, heat shock proteins (HSPs), serine/threonine kinases (STKs), ice-nucleating proteins, membrane protectants, and other similar but less well-characterized proteins serve as prominent cryoprotective agents with unique characteristics and special properties ( Bang et al 2013 , King and MacRae 2015 ). Among these proteins, AFPs have gained much attention because they are known to protect organisms from freezing by lowering the freezing temperature ( T f ) ( Wen et al 2016 ).…”

Frostbite Protection in Mice Expressing an Antifreeze Glycoprotein

“…Anti-freeze glycoproteins (AFGPs), despite being the initially discovered class of AFPs, are significantly less understood than other classes [ 9 , 27 – 29 ]. Their primary amino acid sequence consists of canonical Ala-Ala-Thr or Pro-Ala-Thr repeats with β-D-galactosyl-(1→3)-α-N-acetyl-D-galactosamine disaccharides attached to each threonine [ 27 , 30 ]. Four of these triplet repeats are sufficient for function, and up to 55 repeats have been described in arctic fish AFGPs [ 31 ].…”