Synthetic insect antifreeze peptides modify ice crystal growth habit

Kong, Charles H. Z.; Leung, Ivanhoe K. H.; Sarojini, Vijayalekshmi

doi:10.1039/c7ce00232g

Cited by 5 publications

(5 citation statements)

References 36 publications

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“…The same trends were noticed in glutenin and gliadin. These observations confirmed the ability of these rAFPs to modify ice crystal size, as reported by Kong et al 52 For hydrated gluten, glutenin, and gliadin, rTmAFP was most effective in controlling ice crystals' size, followed by rFiAFP and rCaAFP. Final thawed products quality was closely related to the ice crystals' size formed during freezing.…”

Section: Effects Of Rafps On Water Mobility Of Hydratedsupporting

confidence: 89%

Comparative Study on the Cryoprotective Effects of Three Recombinant Antifreeze Proteins from Pichia pastoris GS115 on Hydrated Gluten Proteins during Freezing

Liu¹,

Liang

Zhang³

et al. 2018

J. Agric. Food Chem.

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During the freezing process, ice crystal formation leads to the deterioration in physicochemical properties and networks of gluten proteins. The cryoprotective effects of recombinant carrot ( Daucus carota) antifreeze protein (rCaAFP), type II antifreeze protein from Epinephelus coioides (rFiAFP), and Tenebrio molitor antifreeze protein (rTmAFP) produced from Pichia pastoris GS115 on hydrated gluten, glutenin, and gliadin during freezing were investigated. The thermal hysteresis (TH) activity and ice crystals' morphology modification ability of recombinant antifreeze proteins (rAFPs) were analyzed by differential scanning calorimetry (DSC) and cryomicroscope, respectively. The freezing and melting properties, water state, rheological properties, and microstructure of hydrated gluten proteins were studied by DSC, low field nuclear magnetic resonance, rheometer, and scanning electron microscopy, respectively. The rTmAFP exhibited strongest TH activity and ice crystals' morphology modification ability, followed by rFiAFP and rCaAFP. The addition of the three rAFPs caused freezing hysteresis and weakened the damage of freezing to the networks of hydrated gluten, glutenin, and gliadin. During freezing, the cryoprotective effects of the three rAFPs on the freezable water content, water mobility and distribution, and rheological properties of hydrated gluten were achieved by protecting these corresponding properties of hydrated glutenin. Among the three rAFPs, rTmAFP was most effective in the cryoprotective activities on hydrated gluten proteins during freezing. The results demonstrate the potential of these rAFPs, especially rTmAFP, to preserve the above properties of hydrated gluten proteins during the freezing process.

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Section: Effects Of Rafps On Water Mobility Of Hydratedsupporting

confidence: 89%

Comparative Study on the Cryoprotective Effects of Three Recombinant Antifreeze Proteins from Pichia pastoris GS115 on Hydrated Gluten Proteins during Freezing

Liu¹,

Liang

Zhang³

et al. 2018

J. Agric. Food Chem.

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“…This observation is in agreement with earlier experimental studies. 46,47 The comparison of the BAI values for Phos and Cit with those of His (see Figure 6 and ref 25), supports our idea that the His buffer features a stronger preference to adsorb on hydrophobic amino acids, in addition to the charged and polar ones. This idea is supported by the generally lower BAI observed for neutral His (His 0 ) across the whole range of amino acids, as represented in Figure 6.…”

Section: Molecular Pharmaceuticssupporting

confidence: 76%

“…We expect that the stronger adsorption on ARG as compared to LYS is facilitated by the interplay between the buffer ion and the guanidinium group of ARG, which can form multiple hydrogen bonds with the buffer ions in addition to electrostatic interaction (see Section for more details). This observation is in agreement with earlier experimental studies. , …”

Section: Resultsmentioning

confidence: 99%

Unraveling the Microscopic Mechanism of Molecular Ion Interaction with Monoclonal Antibodies: Impact on Protein Aggregation

Saurabh,

Zhang,

Seddon

et al. 2024

Mol. Pharmaceutics

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Understanding and predicting protein aggregation represents one of the major challenges in accelerating the pharmaceutical development of protein therapeutics. In addition to maintaining the solution pH, buffers influence both monoclonal antibody (mAb) aggregation in solution and the aggregation mechanisms since the latter depend on the protein charge. Molecular-level insight is necessary to understand the relationship between the buffer−mAb interaction and mAb aggregation. Here, we use all-atom molecular dynamics simulations to investigate the interaction of phosphate (Phos) and citrate (Cit) buffer ions with the Fab and Fc domains of mAb COE3. We demonstrate that Phos and Cit ions feature binding mechanisms, with the protein that are very different from those reported previously for histidine (His). These differences are reflected in distinctive ion-protein binding modes and adsorption/desorption kinetics of the buffer molecules from the mAb surface and result in dissimilar effects of these buffer species on mAb aggregation. While His shows significant affinity toward hydrophobic amino acids on the protein surface, Phos and Cit ions preferentially bind to charged amino acids. We also show that Phos and Cit anions provide bridging contacts between basic amino acids in neighboring proteins. The implications of such contacts and their connection to mAb aggregation in therapeutic formulations are discussed.

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“…The largest chemically synthesized AFPs were based on the structure of the beetle Dendroides canadensis AFP [91]. First, several peptide fragments containing the Cys residues essential for the stability and secondary structure of Dc AFP were synthesized by SPPS.…”

Section: Production Of Af(g)ps and Synthetic Analogues: Design Andmentioning

confidence: 99%

“…Importantly, this approach did not only improve the synthetic yield and purity, but the novel AFPs were also more stable than their natural disulphide bridge containing counterparts. The thermal hysteresis activity of the two constructs was similar, with TH values at a protein concentration of 10 mM between 0.1 and 0.35 °C [91].…”

Section: Production Of Af(g)ps and Synthetic Analogues: Design Andmentioning

confidence: 99%

Peptidic Antifreeze Materials: Prospects and Challenges

Surís-Valls

Voets

2019

IJMS

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Necessitated by the subzero temperatures and seasonal exposure to ice, various organisms have developed a remarkably effective means to survive the harsh climate of their natural habitats. Their ice-binding (glyco)proteins keep the nucleation and growth of ice crystals in check by recognizing and binding to specific ice crystal faces, which arrests further ice growth and inhibits ice recrystallization (IRI). Inspired by the success of this adaptive strategy, various approaches have been proposed over the past decades to engineer materials that harness these cryoprotective features. In this review we discuss the prospects and challenges associated with these advances focusing in particular on peptidic antifreeze materials both identical and akin to natural ice-binding proteins (IBPs). We address the latest advances in their design, synthesis, characterization and application in preservation of biologics and foods. Particular attention is devoted to insights in structure-activity relations culminating in the synthesis of de novo peptide analogues. These are sequences that resemble but are not identical to naturally occurring IBPs. We also draw attention to impactful developments in solid-phase peptide synthesis and ‘greener’ synthesis routes, which may aid to overcome one of the major bottlenecks in the translation of this technology: unavailability of large quantities of low-cost antifreeze materials with excellent IRI activity at (sub)micromolar concentrations.

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Synthetic insect antifreeze peptides modify ice crystal growth habit

Abstract: Synthetic antifreeze peptides based on the hyperactive antifreeze protein modify the shape of ice crystals and show enhanced antifreeze activity with the addition of a small molecule.

Cited by 5 publications

References 36 publications

Comparative Study on the Cryoprotective Effects of Three Recombinant Antifreeze Proteins from Pichia pastoris GS115 on Hydrated Gluten Proteins during Freezing

Comparative Study on the Cryoprotective Effects of Three Recombinant Antifreeze Proteins from Pichia pastoris GS115 on Hydrated Gluten Proteins during Freezing

Unraveling the Microscopic Mechanism of Molecular Ion Interaction with Monoclonal Antibodies: Impact on Protein Aggregation

Peptidic Antifreeze Materials: Prospects and Challenges

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