Graphene oxide destabilizes myoglobin and alters its conformation

Zhu, Zhaohua; Wang, Yanqing; Kang, Yijun; Zhang, Hongmei; Zhang, Zhengming; Fei, Zhenghao; Cao, Jian

doi:10.1016/j.carbon.2016.12.053

Cited by 29 publications

(9 citation statements)

References 46 publications

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“…[10][11][12] In the past few years, graphene oxide with different functionalization and modifications has been extensively investigated to understand its interaction with proteins. [10][11][12][13][14][15] The electrostatic bonding and π-π stacking interactions and covalent/noncovalent bonding are considered to be the major mechanisms of graphene-protein interactions. Graphene-biomolecule interactions have been shown to underpin clinical diagnostic tools for cancer biomarker detection, which demonstrate that graphene-based enzyme modulators are becoming an increasingly relevant alternative to traditional techniques.…”

Section: Introductionmentioning

confidence: 99%

Influence of luminescent graphene quantum dots on trypsin activity

Tabish

Pranjol

Karadag

et al. 2018

IJN

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BackgroundProtein–graphene interactions have the potential to play a pivotal role in the future directions of nanomedicine. These interactions lead to diverse processes such as generation of protein coronas, nano–bio interfaces, particle wrapping, and biocatalytic processes that could determine the ultimate fate of graphene nanocomposites in biologic systems. However, such interactions and their effects on the bioavailability of graphene have not yet been widely appreciated, despite the fact that this is the primary surface in contact with cells.MethodsThis paper reports on the integrative physiochemical interaction between trypsin and graphene quantum dots (GQDs) to determine their potential biologic identity in enzyme engineering. This interaction was measured by a wide range of analytical methods.ResultsDefinitive binding and modulation of trypsin–GQDs was demonstrated for the first time by use of vibrational spectroscopy and wetting transparency, which revealed that trypsin was absorbed on GQDs’ surface through its cationic and hydrophilic residues. Our findings suggested that trypsin’s active sites were stabilized and protected by the GQDs, which were likely to be responsible for the high bioavailability of GQDs in enzymes.ConclusionOur work demonstrates the efficacy of GQDs as an enzyme modulator with high specificity, and their great application potential in enzyme engineering as well as enzyme-based therapies.

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Section: Introductionmentioning

confidence: 99%

Influence of luminescent graphene quantum dots on trypsin activity

Tabish

Pranjol

Karadag

et al. 2018

IJN

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“…CD spectroscopy is an important method for studying the secondary structure of serum albumin 34,37 . As shown in Figure 11C,D, both HSA and BSA show two negative absorption peaks at 208 and 222 nm, which are the characteristic π → π* electronic transitions in the α ‐helical structure of HSA and BSA.…”

Section: Resultsmentioning

confidence: 99%

“…34,35 As shown in CD spectroscopy is an important method for studying the secondary structure of serum albumin. 34,37 As shown in Figure 11C…”

Section: Conformational Variationmentioning

confidence: 87%

Investigations of interaction mechanism and conformational variation of serum albumin affected by artemisinin and dihydroartemisinin

Zhu

Luo

et al. 2022

J of Molecular Recognition

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In this work, binding interactions of artemisinin (ART) and dihydroartemisinin (DHA) with human serum albumin (HSA) and bovine serum albumin (BSA) were investigated thoroughly to illustrate the conformational variation of serum albumin. Experimental results indicated that ART and DHA bound strongly with the site I of serum albumins via hydrogen bond (H-bond) and van der Waals force and subsequently statically quenched the intrinsic fluorescence of serum albumins through concentrationdependent manner. The quenching abilities of two drugs on the intrinsic fluorescence of HSA were much higher than the quenching abilities of two drugs on the intrinsic fluorescence of BSA. Both ART and DHA, especially DHA, caused the conformational variation of serum albumins and reduced the α-helix structure content of serum albumins. DHA with hydrophilic hydroxyl group bound with HSA more strongly, suggesting the important roles of the chemical polarity and the hydrophilicity during the binding interactions of two drugs with serum albumins. These results reveal the molecular understanding of binding interactions between ART derivatives and serum albumins, providing vital information for the future application of ART derivatives in biological and clinical areas.

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“…5c, the myoglobin from rabbit meat has absorption peaks near 411, 537 and 582 nm. The absorption peak at 411 nm is the characteristic absorption peak of haem protein (Zhu et al ., 2017). The absorption peaks at 542 and 581 nm are characteristic absorption peaks of oxymyoglobin (Kim et al ., 2015).…”

Section: Resultsmentioning

confidence: 99%

Effect of multiple freeze‐thaw cycles on protein and lipid oxidation in rabbit meat

Wang

Zhang

et al. 2021

Int J of Food Sci Tech

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Summary Frozen storage is chosen to be the preferred method in meat preservation. However, multiple freeze‐thaw (F‐T) cycles will occur during the transfers or distribution processes under poor cold‐chain conditions. This study investigated the effects of multiple freeze‐thaw (F‐T) cycles on water mobility, microstructure damage, protein oxidation and lipid oxidation in rabbit meat during seven F‐T cycles through 56 days. Scanning electron microscopy results indicated that the increase of F‐T cycles induced the rupture of endomysia and the increase of gaps between fibres. Low‐field nuclear magnetic resonance (LF‐NMR) results showed that the peak area of T21 and T22 decreased with increasing number of repeated F‐T cycles, indicating that immobile water shifted to free water, and free water mobility increased. During repeated freeze‐thaw process, the peroxide value, thiobarbituric acid‐reactive substances, non‐haem iron content and carbonyl groups of rabbit meat gradually increased, whereas haem content, haem iron content and sulfhydryl content of rabbit meat gradually decreased. In addition, the results of Fourier transform infrared, sodium dodecyl sulphate polyacrylamide gel electrophoresis, and intrinsic fluorescence spectroscopy indirectly proved that multiple F‐T cycles could cause α‐helix structure disruption, protein aggregation and degradation, and tryptophan oxidation of rabbit meat myofibrillar protein (MP). Overall, multiple repeated F‐T cycles changed moisture migration, damaged microstructure and promoted lipid and protein oxidation of rabbit meat.

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Graphene oxide destabilizes myoglobin and alters its conformation

Cited by 29 publications

References 46 publications

Influence of luminescent graphene quantum dots on trypsin activity

Influence of luminescent graphene quantum dots on trypsin activity

Investigations of interaction mechanism and conformational variation of serum albumin affected by artemisinin and dihydroartemisinin

Effect of multiple freeze‐thaw cycles on protein and lipid oxidation in rabbit meat

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