<i>Bacopa monnieri</i>inhibit hen egg white lysozyme fibrillation and help in retaining its activity at acidic condition

Varma, Neelakant; Kukrety, Himanshi; Ravi, Vijay; Kumar, Satish

doi:10.1080/07391102.2019.1617784

Cited by 3 publications

(1 citation statement)

References 59 publications

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“…It is thus possible that interaction between negatively charged PVP-AuNP and positively charged HEWL stabilize the protein to retain its activity in presence of sugar. We have earlier demonstrated that chitotriose and brahmi recovers the HEWL activity at pH 12.2 and pH 2 respectively by stabilizing the structure [50,51]. Data obtained from Trp uorescence, circular dichroism and ANS uorescence in association with enzymatic activity strongly advocates that gold nanoparticles stabilize the native structure of HEWL.…”

Section: Pvp-aunp Promote Native Like Structure Of Hewl In Presence O...mentioning

confidence: 96%

PVP-AuNP Impedes Glycation Mediated Hen Egg White Lysozyme Aggregation Under Physiological Condition

Johnson,

Tyagi,

Maity

et al. 2024

BioNanoSci.

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Protein glycation a non-enzymatic protein modi cation, alters the structure of biomolecule leading to several neurodegenerative and other disorders. As onset of disorders due to protein glycation is primarily driven by the development of advanced glycation end products (AGEs), therapeutic intervention against related disorders by inhibiting AGEs production is imperative. Nanoparticles have recently gained more prominence as therapeutic agents in biological eld such as medicine, drug discovery and diagnosis. In present study, we extensively investigated the effect of chemically synthesized polyvinylpyrrolidone conjugated gold nanoparticles (PVP-AuNP) on D-ribose induced glycation of hen egg white lysozyme (HEWL) under physiological conditions. Our nding shows that AGEs formation was inhibited by PVP-AuNP over the period of 20 days. Interaction of gold nanoparticles prevented glycation induced misfolding and aggregation of lysozyme by stabilizing its native structure, which was evident with static light scattering, ThT, Congo red and ANS uorescence coupled with CD spectroscopy. Further, by estimating carbonyl content and thiol group, our study suggests that PVP-AuNP possesses antioxidant property thus prevent the HEWL against glycation driven oxidative damage. Present study therefore elucidates that PVP-AuNP a signi cant antiglycation agent can be used against wide range of disorders induced by AGEs.

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Section: Pvp-aunp Promote Native Like Structure Of Hewl In Presence O...mentioning

confidence: 96%

PVP-AuNP Impedes Glycation Mediated Hen Egg White Lysozyme Aggregation Under Physiological Condition

Johnson,

Tyagi,

Maity

et al. 2024

BioNanoSci.

Self Cite

View full text Add to dashboard Cite

show abstract

Benzoylmesaconine alters the native structure and activity of hen egg white lysozyme: revealing possible mechanism of aconitum-induced toxicity

Marycleopha,

Johnson,

Singh

et al. 2024

Forensic Toxicol

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PVP-AuNP impedes glycation mediated Hen Egg White Lysozyme aggregation under physiological condition

Johnson,

Tyagi,

Maity

et al. 2024

Preprint

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View full text Add to dashboard Cite

Protein glycation a non-enzymatic protein modification, alters the structure of biomolecule leading to several neurodegenerative and other disorders. As onset of disorders due to protein glycation is primarily driven by the development of advanced glycation end products (AGEs), therapeutic intervention against related disorders by inhibiting AGEs production is imperative. Nanoparticles have recently gained more prominence as therapeutic agents in biological field such as medicine, drug discovery and diagnosis. In present study, we extensively investigated the effect of chemically synthesized polyvinylpyrrolidone conjugated gold nanoparticles (PVP-AuNP) on D-ribose induced glycation of hen egg white lysozyme (HEWL) under physiological conditions. Our finding shows that AGEs formation was inhibited by PVP-AuNP over the period of 20 days. Interaction of gold nanoparticles prevented glycation induced misfolding and aggregation of lysozyme by stabilizing its native structure, which was evident with static light scattering, ThT, Congo red and ANS fluorescence coupled with CD spectroscopy. Further, by estimating carbonyl content and thiol group, our study suggests that PVP-AuNP possesses antioxidant property thus prevent the HEWL against glycation driven oxidative damage. Present study therefore elucidates that PVP-AuNP a significant antiglycation agent can be used against wide range of disorders induced by AGEs.

show abstract

Bacopa monnieriinhibit hen egg white lysozyme fibrillation and help in retaining its activity at acidic condition

Cited by 3 publications

References 59 publications

PVP-AuNP Impedes Glycation Mediated Hen Egg White Lysozyme Aggregation Under Physiological Condition

PVP-AuNP Impedes Glycation Mediated Hen Egg White Lysozyme Aggregation Under Physiological Condition

Benzoylmesaconine alters the native structure and activity of hen egg white lysozyme: revealing possible mechanism of aconitum-induced toxicity

PVP-AuNP impedes glycation mediated Hen Egg White Lysozyme aggregation under physiological condition

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