Polycarboxylates enhance beetle antifreeze protein activity

Amornwittawat, Natapol; Wang, Sen; Duman, John G.; Wen, Xin

doi:10.1016/j.bbapap.2008.06.003

Cited by 43 publications

(56 citation statements)

References 39 publications

(61 reference statements)

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“…DAFP-1, the predominant hemolymph AFP of the beetle D. canadensis (including a his-tag), was expressed and purified as previously described (27). Antifreeze glycoproteins were purified from the Antarctic nototheniid toothfish Dissostichus mawsoni.…”

Section: Methodsmentioning

confidence: 99%

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Long-range protein–water dynamics in hyperactive insect antifreeze proteins

Meister

Ebbinghaus

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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233

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Antifreeze proteins (AFPs) are specific proteins that are able to lower the freezing point of aqueous solutions relative to the melting point. Hyperactive AFPs, identified in insects, have an especially high ability to depress the freezing point by far exceeding the abilities of other AFPs. In previous studies, we postulated that the activity of AFPs can be attributed to two distinct molecular mechanisms: (i) short-range direct interaction of the protein surface with the growing ice face and (ii) long-range interaction by protein-induced water dynamics extending up to 20 Å from the protein surface. In the present paper, we combine terahertz spectroscopy and molecular simulations to prove that long-range protein-water interactions make essential contributions to the high antifreeze activity of insect AFPs from the beetle Dendroides canadensis. We also support our hypothesis by studying the effect of the addition of the osmolyte sodium citrate.hydration dynamics | THz spetroscopy A ntifreeze proteins (AFPs) and antifreeze glycoproteins (AFGPs) are classes of proteins that suppress ice growth in organisms and thereby enable their survival in subfreezing habitats (1). Despite their similar function, many distinct structures have been identified so far. AFPs have been identified in several organisms, including polar fish (2), insects (3), bacteria (4), and plants (5). Their common characteristic is the depression of the freezing temperatures of ice growth of a solution without depressing the melting point equilibrium of protein solutions. This nonequilibrium phenomenon leads to a difference between the freezing and melting temperature, which is referred to as thermal hysteresis (TH). TH is used as a characteristic measure for antifreeze activity of an AFP (6). AFGPs and AFPs, as extracted from the blood of polar fish, usually exhibit up to 2°of TH activity and are termed moderately active AFPs, whereas insect AFPs can exhibit over 5°of TH and therefore, are referred to as hyperactive AFPs. The work by Raymond and DeVries (7,8) proposed a mechanism in which freezing point depression is achieved by an adsorption-inhibition mechanism, in which the proteins recognize and bind "quasiirreversibly" to an ice surface, thereby preventing growth of ice crystals. The adsorption of the protein is thought to prevent macroscopic ice growth in the hysteresis gap, but microscopic growth occurs at the interface in the form of highly curved fronts between adsorbed antifreeze molecules. This effect will cause a decrease of the local freezing temperature because of the Kelvin effect, while leaving the melting temperature relatively unaffected (7). As recently pointed out in the work by Sharp (9), antifreeze activity involves one of the most difficult recognition problems in biology, the distinction between water as liquid and ice. The initially proposed mechanism builds on a local mechanism. In particular, threonine (Thr) residues were proposed to play a decisive role: their hydroxyl groups were thought to be responsible for the high af...

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Section: Methodsmentioning

confidence: 99%

“…AFPs show an increased activity on the addition of osmolytes (26,27). The molecular mechanism for this increase is still a matter of discussion.…”

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confidence: 99%

Long-range protein–water dynamics in hyperactive insect antifreeze proteins

Meister

Ebbinghaus

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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233

221

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“…Trisodium citrate was reported as one of the strong enhancers of antifreeze activity in terms of both TH and ice crystal growth modification. 30 Citrate also causes the highest increase in the TH of insect AFPs. 28 The addition of citrate noticeably increased the activity of the DCR analogues (DCR26, DCR39, DCR26 cyclic and DCR39 cyclic), not only promoting extreme crystal shaping resembling the very small ice crystals produced by the native DcAFP protein, but also creating a significant increase in TH (Fig.…”

mentioning

confidence: 99%

Synthetic insect antifreeze peptides modify ice crystal growth habit

2017

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“…The Hoffmeister effect may be responsible for enhancement of TH by monovalent salts (Wang et al, 2009a). Increasing numbers of hydroxyl groups in a series of polycarboxylates (Amornwittawat et al, 2008) and polyhydroxy compound enhancers (Amornwittawat et al, 2009) positively affected the TH of DAFP-1. Arginine is a key residue in the enhancement (Wang et al, 2009b).…”

Section: Dendroides Canadensis Beetlesmentioning

confidence: 99%

Animal ice-binding (antifreeze) proteins and glycolipids: an overview with emphasis on physiological function

Duman¹

2015

Journal of Experimental Biology

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133

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Ice-binding proteins (IBPs) assist in subzero tolerance of multiple cold-tolerant organisms: animals, plants, fungi, bacteria etc. IBPs include: (1) antifreeze proteins (AFPs) with high thermal hysteresis antifreeze activity; (2) low thermal hysteresis IBPs; and (3) icenucleating proteins (INPs). Several structurally different IBPs have evolved, even within related taxa. Proteins that produce thermal hysteresis inhibit freezing by a non-colligative mechanism, whereby they adsorb onto ice crystals or ice-nucleating surfaces and prevent further growth. This lowers the so-called hysteretic freezing point below the normal equilibrium freezing/melting point, producing a difference between the two, termed thermal hysteresis. True AFPs with high thermal hysteresis are found in freeze-avoiding animals (those that must prevent freezing, as they die if frozen) especially marine fish, insects and other terrestrial arthropods where they function to prevent freezing at temperatures below those commonly experienced by the organism. Low thermal hysteresis IBPs are found in freeze-tolerant organisms (those able to survive extracellular freezing), and function to inhibit recrystallization -a potentially damaging process whereby larger ice crystals grow at the expense of smaller ones -and in some cases, prevent lethal propagation of extracellular ice into the cytoplasm. Ice-nucleator proteins inhibit supercooling and induce freezing in the extracellular fluid at high subzero temperatures in many freeze-tolerant species, thereby allowing them to control the location and temperature of ice nucleation, and the rate of ice growth. Numerous nuances to these functions have evolved. Antifreeze glycolipids with significant thermal hysteresis activity were recently identified in insects, frogs and plants.

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Polycarboxylates enhance beetle antifreeze protein activity

Cited by 43 publications

References 39 publications

Long-range protein–water dynamics in hyperactive insect antifreeze proteins

Long-range protein–water dynamics in hyperactive insect antifreeze proteins

Synthetic insect antifreeze peptides modify ice crystal growth habit

Animal ice-binding (antifreeze) proteins and glycolipids: an overview with emphasis on physiological function

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