Conformations of Oxidized Glutathione in Aqueous Urea Solution by All-Atom Molecular Dynamic Simulations and 2D-NOESY Spectrum

Zhang, Rong; Huang, Guangqing; Zeng, Wei; Wu, Wenjuan

doi:10.1007/s10953-013-0097-4

Cited by 6 publications

(6 citation statements)

References 43 publications

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“…It indicates that the two amino acids are relatively flexible and exhibit an extended conformation in aqueous solution. 30 The structure of the peptide is loosely extended so that the active site of the side chain is exposed and could interact with the natural substrate. The moiety extended structure by amino acid may interact with several enzyme sites (AChE) through hydrogen bonds and van der Waals interactions.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…The presence of the NOE effect, which represents close contacts between protons in space, can be verified by the absence of short-range coupling signals. It indicates that the two amino acids are relatively flexible and exhibit an extended conformation in aqueous solution . The structure of the peptide is loosely extended so that the active site of the side chain is exposed and could interact with the natural substrate.…”

Section: Results and Discussionmentioning

confidence: 99%

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Neuroprotective Function of a Novel Hexapeptide QMDDQ from Shrimp via Activation of the PKA/CREB/BNDF Signaling Pathway and Its Structure–Activity Relationship

Zhang

Sun

et al. 2020

J. Agric. Food Chem.

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This study aimed to evaluate the neuroprotective function of shrimp-derived peptides QMDDQ and KMDDQ. Biochemical results revealed that both peptides exhibited neuroprotective effects by increasing acetylcholine (ACh) content and inhibiting acetylcholinesterase (AChE) activity in PC12 cells; QMDDQ was more active than KMDDQ. COSY–NOESY spectroscopic data showed that the superior neuroprotective function of QMDDQ might be attributed to its N-terminal glutamine as it exhibited an extended spatial conformation, facilitating its interactions with AChE. QMDDQ can promote the basic energy metabolism of cells more than KMDDQ. The peptides showed neuroprotective ability due to the activation of the antiapoptosis and PKA/CREB/BNDF signaling pathway. QMDDQ was selected to investigate its memory-enhancing activity in scopolamine-induced amnesic mice, revealing memory protection in mice, as it improved their performance in the Morris water maze experiment. In addition, QMDDQ increased ACh content (4.98 ± 0.51 μg/mg prot) and decreased AChE activity (4.72 ± 0.11 U/mg prot) in the mouse hippocampus. These data indicate the systemic mechanism through which naturally derived QMDDQ improved neuroprotection and memory ability.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Section: Results and Discussionmentioning

confidence: 99%

Neuroprotective Function of a Novel Hexapeptide QMDDQ from Shrimp via Activation of the PKA/CREB/BNDF Signaling Pathway and Its Structure–Activity Relationship

Zhang

Sun

et al. 2020

J. Agric. Food Chem.

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“…In D 2 O solution, the LAP-I showed three NOE signals, including Lys-H β and Val-H γ , Phe-H β2 and Lys-H β , and Ala-H β and Ile-H δ2 . None of these three NOE signals were attached to the same C atom, indicating the compact stretch state of LAP-I in D 2 O [48,49]. LAP-II showed six NOE signals, including Ala-H β and Val-H γ , Leu-H β and Val-H γ , Cys-H β and Leu-H β , Cys-H β and Glu-H β , Pro-H δ2 and Gln-H β , and Pro-H δ1 and Pro-H δ2 .…”

Section: D-nmr Analysismentioning

confidence: 97%

“…LAP-II showed six NOE signals, including Ala-H β and Val-H γ , Leu-H β and Val-H γ , Cys-H β and Leu-H β , Cys-H β and Glu-H β , Pro-H δ2 and Gln-H β , and Pro-H δ1 and Pro-H δ2 . The hydrogen atoms Pro-H δ1 and Pro-H δ2 produced NOE signals with each other, indicating the "folded" state in LAP-II [48,49]. Different substances exhibit different states in water due to the properties of the substances.…”

Section: D-nmr Analysismentioning

confidence: 98%

“…Different substances exhibit different states in water due to the properties of the substances. It might be attributed to the fact that the two chains connected by the disulfide linkage of the peptide molecules exhibit different flexibilities in water [48]. Qi et al [49] reported that GEF (Gly Glu Phe) usually exists in a stretched state in water.…”

Section: D-nmr Analysismentioning

confidence: 99%

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Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates

Mao

Yun

et al. 2023

Molecules

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Loach, rich in nutrients, such as proteins, amino acids, and mineral elements, is being gradually favored by consumers. Therefore, in this study, the antioxidant activity and structural characteristics of loach peptides were comprehensively analyzed. The loach protein (LAP) with a molecular weight between 150 and 3000 Da was graded by ultrafiltration and nanofiltration processes, which exhibited excellent scavenging activity against DPPH radical (IC50 2.91 ± 0.02 mg/mL), hydroxyl radical (IC50 9.95 ± 0.03 mg/mL), and superoxide anion radical (IC50 13.67 ± 0.33 mg/mL). Additionally, LAP was purified by gel filtration chromatography, and two principal components (named as LAP-I and LAP-II) were isolated. A total of 582 and 672 peptides were identified in LAP-I and LAP-II, respectively, through structural analysis. The XRD results revealed that LAP-I and LAP-II had an irregular amorphous structure. The 2D-NMR spectroscopy results suggested that LAP-I had a compact stretch conformation in the D2O solution, while LAP-II had a folded conformation. Overall, the study results suggested that loach peptide could be a potential antioxidant agent and might provide valuable information for chain conformation and antioxidant mechanism research further.

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Deciphering the Conformations of Glutathione Oxidized Peptide: A Comparative NMR Study in Solution and Solid‐State Environments

Senapati,

Yarava,

Ramanathan

et al. 2024

Magnetic Reson in Chemistry

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Glutathione (GSH) and its oxidized dimer (GSSG) play an important role in living systems as an antioxidant, balancing the presence of reactive oxygen species (ROS). The central thiol (‐S‐S‐) bond in GSSG can undergo free rotation, providing multiple conformations with respect to the S‐S bridge. The six titratable sites of GSSG, which are influenced by pH variations, affect these conformations in solution, whereas in solids, additionally crystal packing effects come into play. In view of differing reports about the structure of GSSG in literature, we have here conducted an extensive reexamination of its conformations using NMR, and contrasting results have been obtained for solution and solid state. In solution, the existence of more than one antiparallel orientation of the monomer unit with different hydrogen bonding schemes has been indicated by NOE and amide temperature coefficient results. On the other hand, in the solid‐state, a 1H‐1H double‐quantum (DQ) to 13C single‐quantum (SQ) correlation study has confirmed a parallel orientation, consistent with the reported X‐ray crystal structure. Experimentally assigned solid‐state NMR resonances have been validated using GIPAW calculations incorporated in the Quantum ESPRESSO package.

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Conformations of Oxidized Glutathione in Aqueous Urea Solution by All-Atom Molecular Dynamic Simulations and 2D-NOESY Spectrum

Cited by 6 publications

References 43 publications

Neuroprotective Function of a Novel Hexapeptide QMDDQ from Shrimp via Activation of the PKA/CREB/BNDF Signaling Pathway and Its Structure–Activity Relationship

Neuroprotective Function of a Novel Hexapeptide QMDDQ from Shrimp via Activation of the PKA/CREB/BNDF Signaling Pathway and Its Structure–Activity Relationship

Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates

Deciphering the Conformations of Glutathione Oxidized Peptide: A Comparative NMR Study in Solution and Solid‐State Environments

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