Antifreeze Glycoproteins: Elucidation of the Structural Motifs That Are Essential for Antifreeze Activity

Tachibana, Yuki; Fletcher, George P.; Fujitani, Naoki; Tsuda, Sakae; Monde, Kenji; Nishimura, Shin‐Ichiro

doi:10.1002/ange.200353110

Cited by 71 publications

(159 citation statements)

References 33 publications

Supporting

Mentioning

145

Contrasting

Order By: Relevance

“…Several ion peaks shown in Figure 4 a . Surprisingly, it also appears that the minimal active structure of the antifreeze glycopeptide (syAFGP 3 ) [7] forms specific complexes with three water molecules as shown in Figure 5, whereas the inactive monomeric AFGP (syAFGP 1 ) produced neither the complex with water nor the selfaggregation behavior found with the Le X trisaccharide. …”

mentioning

confidence: 89%

“…Such valuable information could not be obtained by common ESI-TOF MS techniques carried out at 200 8C as shown in Figure 2 b. Moreover, when a compound library void of chitooligosaccharides was assayed at 4 8C, lysozyme showed significant affinity toward the maltooligosaccharides (d-glucose) [3][4][5][6][7] and g-cyclodextrin. These interactions cannot be detected by general spectroscopic analyses such as UV/Vis, fluorometric, and SPR methods.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Direct Observation of Sugar–Protein, Sugar–Sugar, and Sugar–Water Complexes by Cold‐Spray Ionization Time‐of‐Flight Mass Spectrometry

et al. 2005

Self Cite

View full text Add to dashboard Cite

The direct observation of noncovalent and specific intermolecular-recognition events such as enzyme-substrate, antigenantibody, receptor-ligand, carbohydrate-protein, and carbohydrate-carbohydrate interactions is important for understanding the mechanisms behind these biological processes. Electrospray ionization mass spectrometry (ESI MS) is an important tool for investigations of the sensitivity, specificity, and speed of noncovalent complex formation.[1] The advantages of MS over traditional methods such as UV/Vis spectroscopy, fluorescence spectroscopy, surface plasmon resonance (SPR), isothermal titration microcalorimetry, NMR spectroscopy, and X ray crystallographic analysis include the accuracy of mass measurement, speed of analysis, and small sample quantities. However, the harsh conditions of the ionization process in MS are often detrimental to the survival of noncovalent and unstable biomolecular interactions such as those of sugar-protein, sugar-sugar, and sugarwater complexes. Recently, Yamaguchi and co-workers developed cold-spray ionization mass spectrometry (CSI MS), which allows facile and precise characterization of labile self-assembling nanostructures and unstable organometallic complexes in solution.[2] CSI MS may become one of the most promising and versatile tools for characterizing a variety of weak but specific biomolecular interactions, as the ionization at low temperature (À20 8C) allows direct observation of unstable large-scale aggregates of amino acids or nucleosides in organic solvents with magnetic-sector-equipped instruments.[2d, e] It was suggested that a cooled ion spray promotes stable solvation-ionization processes through increased compound polarizability caused by higher dielectric constants at low temperature. Moreover, CSI MS combined with an orthogonal acceleration time-of-flight (oa-TOF) mass analyzer extends the applicability of this method to the characterization of dynamic interactions of biomacromolecules. This is possible through a number of attractive features of TOF MS analyzers, such as their theoretically unlimited mass range, very high spectrum acquisition rates, high ion transmission, high sensitivity, multiplex detection capacity, reasonable mass resolution, and simplicity in instrument design. Our interest is focused on the potential of CSI-TOF MS, with particular respect to specific and weak biomolecular interactions in water at low temperature. Herein we report the feasibility of the CSI-TOF MS method to monitor directly the formation of noncovalent proteincarbohydrate, carbohydrate-carbohydrate, and carbohydrate-water complexes in aqueous solution at 4 8C. Figure 1 a shows the effect of temperature on complex formation between hen egg lysozyme and the chitooligosaccharide, chitotetraose. As anticipated, the intensity of the signal that corresponds to the lysozyme-chitotetraose complex as the major hydrolytic product was gradually enhanced by lowering the ion spray temperature of the reaction mixture from 200 to 4 8C. As shown in Figure 1 b, CSI-TOF MS is ...

show abstract

mentioning

confidence: 89%

mentioning

confidence: 99%

Direct Observation of Sugar–Protein, Sugar–Sugar, and Sugar–Water Complexes by Cold‐Spray Ionization Time‐of‐Flight Mass Spectrometry

et al. 2005

Self Cite

View full text Add to dashboard Cite

show abstract

“…[ 14 ] Furthermore, minor changes in the confi guration of the sugar moiety, and the presence of acetyl or methyl groups can signifi cantly alter the antifreeze activity. [ 15,16 ] The effect of molecular weight on the ice recrystallization inhibition (IRI) activity of PVA has been well described by Congdon et al [ 6 ] One unexplored research direction is the effect of main chain architecture on the IRI activity of PVA. Over the past two decades, advances in polymer sciences in living/controlled radical polymerization techniques have led to the design and synthesis of novel macromolecular architectures, such as block copolymers, branched and dendritic polymers, molecular bottlebrushes, etc.…”

Section: Introductionmentioning

confidence: 99%

Influence of Polymer Chain Architecture of Poly(vinyl alcohol) on the Inhibition of Ice Recrystallization

Olijve

Hendrix

Voets

2016

Macromol. Chem. Phys.

View full text Add to dashboard Cite

Poly(vinyl alcohol) (PVA) is a water‐soluble synthetic polymer well‐known to effectively block the recrystallization of ice. The effect of polymer chain architecture on the ice recrystallization inhibition (IRI) by PVA remains unexplored. In this work, the synthesis of PVA molecular bottlebrushes is described via a combination of atom‐transfer radical polymerization and reversible addition‐fragmentation chain‐transfer polymerization. The facile preparation of the PVA bottlebrushes is performed via the selective hydrolysis of the chloroacetate esters of the poly(vinyl chloroacetate) (PVClAc) side chains of a PVClAc precursor bottlebrush. The IRI efficacy of the PVA bottlebrush is quantitatively compared to linear PVA. The results show that even if the PVA chains are densely grafted onto a rigid polymer backbone, the IRI activity of PVA is maintained, demonstrating the flexibility in PVA polymer chain architecture for the design of synthetic PVA‐based ice growth inhibitors.

show abstract

“…The first synthesis of AFGPs as pure glycoforms was reported by Nishimura and colleagues in 2004, [30] in a landmark paper that also reported the first structure-activity studies on AFGPs, and thus provided data that are essential to understanding the mechanism of action and to guiding the design of AFGP mimics. This paper followed an early communication that demonstrated that polymeric AFGP of molecular weight (MW) = 6000-7000 could be efficiently synthesised by simple polymerisation of the repeating glycopeptide unit of AFGP with diphenylphosphoryl azide (DPPA) as a promoter.…”

Section: Natural Antifreeze Glycoproteinsmentioning

confidence: 96%

“…[32] The overall synthesis is shown in Scheme 2. [30] Building block 1 was produced by glycosidation of Ala-Thr-Ala with an orthogonally protected disaccharide followed by deprotection. With DPPA as the promoter, polymerisation of 1 produced a mixture of glycoforms containing 8-15 repeating units, while using a lower temperature and shorter reaction times resulted in low-MW fractions containing between two and eight repeatScheme 1.…”

Section: Natural Antifreeze Glycoproteinsmentioning

confidence: 99%

Design and Synthesis of Antifreeze Glycoproteins and Mimics

Harding

2010

ChemBioChem

View full text Add to dashboard Cite

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.

show abstract

Antifreeze Glycoproteins: Elucidation of the Structural Motifs That Are Essential for Antifreeze Activity

Cited by 71 publications

References 33 publications

Direct Observation of Sugar–Protein, Sugar–Sugar, and Sugar–Water Complexes by Cold‐Spray Ionization Time‐of‐Flight Mass Spectrometry

Direct Observation of Sugar–Protein, Sugar–Sugar, and Sugar–Water Complexes by Cold‐Spray Ionization Time‐of‐Flight Mass Spectrometry

Influence of Polymer Chain Architecture of Poly(vinyl alcohol) on the Inhibition of Ice Recrystallization

Design and Synthesis of Antifreeze Glycoproteins and Mimics

Contact Info

Product

Resources

About