Effects of interaction with gene carrier polyethyleneimines on conformation and enzymatic activity of pig heart lactate dehydrogenase

Wang, Fan; Mo, Junyong; Huang, Aimin; Zhang, Min; Ma, Lin

doi:10.1016/j.saa.2018.06.048

Cited by 6 publications

(26 citation statements)

References 51 publications

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“… 15 , 16 The secondary structure estimation by the CDSSTR method 17 indicated 40% α-helices, 12% β-sheets, 14% β-turn, and 34% random coil for rmLDH in the absence of PEI, approximate to those of pgLDH from our previous work. 9 PEI addition resulted in a transition from α-helix to β-sheet and random coil ( Table 1 ), indicating a less ordered conformation of rmLDH. The result was opposite to that of phLDH, suggesting a difference in the interaction with PEI.…”

Section: Resultsmentioning

confidence: 99%

“…As an extension of the previous work, 9 the conformational change of rabbit muscle LDH (rmLDH, a basic protein with pI ∼ 8.2) 6 in the solutions containing PEI of typical molecular weights 25,000 and 1800 Da (labeled as PEI25k and PEI1.8k, respectively.) was investigated by UV–vis absorption, resonance Rayleigh scattering (RRS), fluorescence, and circular dichroism (CD).…”

Section: Introductionmentioning

confidence: 81%

“…Previous work from our group suggested that hydrophobic interaction and hydrogen bond dominated the surface binding of PEI on horseradish peroxidase (HRP, a neutral protein of pI ∼ 7.0) and pig heart LDH (phLDH, an acid protein of pI ∼ 5.6), 6 leading to a more compact conformation. 8 , 9 …”

Section: Introductionmentioning

confidence: 99%

“…Enzymatic activity of rmLDH was also monitored by the catalytic reduction of sodium pyruvate to lactate using β-nicotinamide adenine dinucleotide (NADH) as the coenzyme. A comparison was made to the effects of PEI on the conformation and biofunction of rmLDH and phLDH, 9 with the purpose to have a better understanding on the mechanism of PEI–protein interaction.…”

Section: Introductionmentioning

confidence: 99%

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Conformational Change and Activity Enhancement of Rabbit Muscle Lactate Dehydrogenase Induced by Polyethyleneimine

Ren

et al. 2021

ACS Omega

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For a better understanding on the interaction between polyethyleneimine (PEI) and proteins, spectroscopic studies including UV–vis absorption, resonance Rayleigh scattering, fluorescence, and circular dichroism were conducted to reveal the conformational change of rabbit muscle lactate dehydrogenase (rmLDH) and related to the bioactivity of the enzyme. Regardless of the electrostatic repulsion, PEI could bind on the surface of rmLDH, a basic protein, via hydrogen binding of the dense amine groups and hydrophobic interaction of methyl groups. The competitive binding by PEI led to a reduction of the binding efficiency of rmLDH toward β-nicotinamide adenine dinucleotide, the coenzyme, and sodium pyruvate, the substrate. However, the complex formation with PEI induced a less ordered conformation and an enhanced surface hydrophobicity of rmLDH, facilitating the turnover of the enzyme and generally resulting in an increased activity. PEI of higher molecular weight was more efficient to induce alteration in the conformation and catalytic activity of the enzyme.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 81%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Conformational Change and Activity Enhancement of Rabbit Muscle Lactate Dehydrogenase Induced by Polyethyleneimine

Ren

et al. 2021

ACS Omega

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“…This was also observed in hydra exposed to NPs where a 0.15 decrease in the fD was associated with a circa 2.5-fold increase in the amplitude in viscosity waves. The LDH enzyme complex oscillated between a relaxed and tensed state during its activity but at time scales of 260 µsec [ 22 ]. The bimolecular rate process occurring at different time scales (nsec–usec) indicates a complex dynamical structure of the substrates binding process.…”

Section: Discussionmentioning

confidence: 99%

Crowding Effects of Polystyrene Nanoparticles on Lactate Dehydrogenase Activity in Hydra Attenuata

Auclair

Gagné

2020

JoX

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Plastics pervade our environment and potentially release important quantities of plastic nanoparticles (NPs) from degradation in the environment. The purpose of this study was to examine the crowding effects of polystyrene NPs on lactate dehydrogenase (LDH) in vitro and following exposure to Hydra attenuata. First, LDH activity was measured in vitro in the presence of filamentous (F-)actin and NPs (50 and 100 nm diameter) to determine changes in viscosity and the fractal kinetics of LDH. The fractal dimension (fD) was also determined using the rescaled range analysis procedure. Secondly, these changes were examined in hydra exposed to NPs for 96h to concentrations of NPs. The data revealed that the addition of F-actin increased the rate of LDH at low substrate (pyruvate) concentrations compared to LDH alone with a gradual decrease in the rate with the addition of pyruvate, which is characteristic of the fractal behavior of enzymes in crowded environments. The addition of 50 and 100 nm NPs also produced these changes, which suggest that NPs could change the space properties of the LDH reaction. The fD was reduced to 0.85 and 0.91 with 50 and 100 nm NPs compared to 1.093 with LDH alone. Decrease in the fD was related with increased amplitudes and frequency in viscosity waves in the reaction media. Exposure of hydra to NPs confirmed the increase in LDH activity and the fD was significantly correlated with LDH activity (r = −0.5). Correction of LDH activity (residuals) still revealed an increase in LDH activity in hydra suggesting increased anaerobic metabolism by NPs. In conclusion, the presence of NPs in the intracellular space decreased the fD, which could influence LDH activity in organisms exposed to NPs.

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Exploring the therapeutic potential of rutin through investigating its inhibitory mechanism on lactate dehydrogenase: Multi-spectral methods and computer simulation

Ding,

Yang,

Wang

et al. 2024

Bioorganic Chemistry

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Effects of interaction with gene carrier polyethyleneimines on conformation and enzymatic activity of pig heart lactate dehydrogenase

Cited by 6 publications

References 51 publications

Conformational Change and Activity Enhancement of Rabbit Muscle Lactate Dehydrogenase Induced by Polyethyleneimine

Conformational Change and Activity Enhancement of Rabbit Muscle Lactate Dehydrogenase Induced by Polyethyleneimine

Crowding Effects of Polystyrene Nanoparticles on Lactate Dehydrogenase Activity in Hydra Attenuata

Exploring the therapeutic potential of rutin through investigating its inhibitory mechanism on lactate dehydrogenase: Multi-spectral methods and computer simulation

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