Blood glycoprotein from antarctic fish possible conformational origin of antifreeze activity

Franks, Felix; Morris, Edwin R.

doi:10.1016/0304-4165(78)90148-4

Cited by 52 publications

(28 citation statements)

References 30 publications

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“…All of our data indicate that the active AFGP has some partially extended conformation. We have recently proposed a 3-fold left-handed helical model (58) which also agrees with the general tenure of the data of Franks & Morris (59). The unusual circular dichroism structure of the peptide chain of AFGP is seen in Fig.…”

supporting

confidence: 83%

Penguin egg‐white and polar fish blood‐serum proteins

Feeney

1982

International Journal of Peptide and Protein Research

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The development of, and findings in, a long-term research program on penguin proteins and polar fish blood proteins are described. Two of the egg-white proteins from the Adelie penguin (Pygoscelis adeliue) have unique properties: a glycoprotein named penalbumin that is a major constituent with some characteristics similar t o ovalbumin, and an ovomucoid with strong inhibitory capacity for subtilisin as well as for bovine trypsin and achymotrypsin. The antifreeze glycoproteins from Antarctic fish (Trematomus borchgrevinki and Dissostichus mawsoni) and an Arctic fish (Boreogadus saida) appear to function noncolligatively by lowering the freezing temperature without affecting the melting point. Current evidence indicates that the antifreeze glycoprotein functions at the ice-solution interface, either on the ice surface or in a transition layer between the solution and the ice.

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confidence: 83%

Penguin egg‐white and polar fish blood‐serum proteins

Feeney

1982

International Journal of Peptide and Protein Research

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“…The lack of a sharp transition in the spectra was consistent with an unordered conformation in solution. Independent CD studies [83], quasielastic light scattering [84] and Raman spectroscopy measurements [85] all suggested the presence of some folded structure.…”

Section: Solution Conformationmentioning

confidence: 99%

‘Antifreeze’ glycoproteins from polar fish

Harding

Anderberg

Haymet

2003

European Journal of Biochemistry

255

200

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Antifreeze glycoproteins (AFGPs) constitute the major fraction of protein in the blood serum of Antarctic notothenioids and Arctic cod. Each AFGP consists of a varying number of repeating units of (Ala-Ala-Thr) n , with minor sequence variations, and the disaccharide b-D-galactosyl-(1fi3)-a-N-acetyl-D-galactosamine joined as a glycoside to the hydroxyl oxygen of the Thr residues. These compounds allow the fish to survive in subzero ice-laden polar oceans by kinetically depressing the temperature at which ice grows in a noncolligative manner. In contrast to the more widely studied antifreeze proteins, little is known about the mechanism of ice growth inhibition by AFGPs, and there is no definitive model that explains their properties. This review summarizes the structural and physical properties of AFGPs and advances in the last decade that now provide opportunities for further research in this field.High field NMR spectroscopy and molecular dynamics studies have shown that AFGPs are largely unstructured in aqueous solution. While standard carbohydrate degradation studies confirm the requirement of some of the sugar hydroxyls for antifreeze activity, the importance of following structural elements has not been established: (a) the number of hydroxyls required, (b) the stereochemistry of the sugar hydroxyls (i.e. the requirement of galactose as the sugar), (c) the acetamido group on the first galactose sugar, (d) the stereochemistry of the b-glycosidic linkage between the two sugars and the a-glycosidic linkage to Thr, (e) the requirement of a disaccharide for activity, and (f) the Ala and Thr residues in the polypeptide backbone. The recent successful synthesis of small AFGPs using solution methods and solidphase chemistry provides the opportunity to perform key structure-activity studies that would clarify the important residues and functional groups required for activity.Genetic studies have shown that the AFGPs present in the two geographically and phylogenetically distinct Antarctic notothenioids and Arctic cod have evolved independently, in a rare example of convergent molecular evolution. The AFGPs exhibit concentration dependent thermal hysteresis with maximum hysteresis (1.2°C at 40 mgAEmL )1 ) observed with the higher molecular mass glycoproteins. The ability to modify the rate and shape of crystal growth and protect cellular membranes during lipid-phase transitions have resulted in identification of a number of potential applications of AFGPs as food additives, and in the cryopreservation and hypothermal storage of cells and tissues.

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“…[53][54] However, contradictory conclusions regarding the solution conformation arose from using different techniques. While early studies concluded that AFGPs adopt predominantly a random-coil conformation, [14,[55][56] later reports suggested a more ordered helical structure. [54,[57][58] High-field NMR studies [59][60] of AFGP1-5, which vary in length from 60-120 residues, showed no evidence for a rigid or well-defined structure in solution even near the freezing temperature of water.…”

Section: Conformational Analysismentioning

confidence: 99%

Design and Synthesis of Antifreeze Glycoproteins and Mimics

Harding

2010

ChemBioChem

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Antifreeze glycoproteins are an important class of biological antifreezes that have potential applications in many areas of medicine, agriculture and industry in which ice crystal growth is damaging. While the synthesis of antifreeze glycoproteins as pure glycoforms has recently been achieved by using ligation and polymerisation strategies, the routine production of large quantities of pure glycoforms remains challenging. A range of C-linked analogues that are readily produced by solid-phase synthesis have delivered novel compounds that are not biological antifreezes, but are potent, non-cytotoxic, ice-recrystallisation inhibitors. Structure-activity studies, the identification of cyclic antifreeze glycoproteins and conformational studies have provided further insight into the requirements for antifreeze activity. These results, coupled with significant advances in approaches to the routine synthesis of different glycoproteins and mimics, present opportunities for the design and synthesis of novel ice-growth-inhibiting and antifreeze compounds.

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Blood glycoprotein from antarctic fish possible conformational origin of antifreeze activity

Cited by 52 publications

References 30 publications

Penguin egg‐white and polar fish blood‐serum proteins

Penguin egg‐white and polar fish blood‐serum proteins

‘Antifreeze’ glycoproteins from polar fish

Design and Synthesis of Antifreeze Glycoproteins and Mimics

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