In Silico Elucidation of the Binding Mechanisms and Molecular Dynamics of Oroxylin A -2,3-Dioxygenase Interaction: An Insight into Therapeutic Potentiation of Quercetin’s Cardioprotection.

Azizeh Shadidizaji; Kağan Tolga Cinisli; Mohamad Warda; Öznur Altunlu; Sahar Memarkashani; Farideh Ghalamfarsa; Abdullah Menzek; Dilanur Ateş

Makale detayları

In Silico Elucidation of the Binding Mechanisms and Molecular Dynamics of Oroxylin A -2,3-Dioxygenase Interaction: An Insight into Therapeutic Potentiation of Quercetin’s Cardioprotection.

Yazarlar:

Azizeh Shadidizaji | Kağan Tolga Cinisli | Mohamad Warda | Öznur Altunlu | Sahar Memarkashani | Farideh Ghalamfarsa | Abdullah Menzek | Dilanur Ateş

Yayıncı:

Ataturk University

Ana Başlıklar:

Biological Psychology (Other)

Dergi:

Recent Trends in Pharmacology Vol.2 Issue 1, pp.27-35

Belge Tipi:

Makale

Yayın Tarihi:

3/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001317055

pISSN:

2980-194X

Anahtar kelimeler:

Özet:

 Elucidating the intricate interplay between enzymes and natural compounds is essential for designing therapeutic strategies. This study employs advanced computational techniques to explore the binding mechanisms between quercetin 2,3-dioxygenase QDO and oroxylin A, revealing specific interaction patterns and key residues crucial to the formation of the QDO-oroxylin A complex. Molecular docking simulations revealed a favorable binding affinity docking score: -5.6 kcalmol between Oroxylin A and the active site cavity of QDO, which was supported by Oroxylin As specific orientation Pose 3. Despite an observed RMSD value of 2.776 indicating a moderate deviation between the docked pose and the reference structure, the formation of two hydrogen bonds with GLN 93 chain D underscores specific molecular interactions driving the binding process. This hydrogen bond formation suggested the presence of a stable and specific binding mode between Oroxylin A and QDO, likely influencing the functional dynamics of the enzyme, necessitating further refinement and validation of the docking model. The ensuing deliberation on the implications of Oroxylin A include its potential as a modulator of QDO activity, emphasizing the importance of molecular-level insights in comprehending enzyme-compound interactions. Oroxylin A, a quercetin 2,3-dioxygenase inhibitor, was used in combination with other agents to prolong the biological impacts of quercetin, thereby amplifying its antioxidant and anti-inflammatory effects. This strategic approach exhibits promise in augmenting cardioprotective benefits, immune system support, and protection against diverse pathological conditions. Subsequent considerations of dosage, bioavailability, and healthcare professional consultation are imperative for judicious supplementation, particularly in individuals with prevailing health conditions or medications. This ongoing in silico study is dedicated to revealing the potential synergistic interactions of Oroxylin A, potentiating the long-term effects of quercetin and advancing our understanding of these intricacies.

 Elucidating the intricate interplay between enzymes and natural compounds is essential for designing therapeutic strategies. This study employs advanced computational techniques to explore the binding mechanisms between quercetin 2,3-dioxygenase QDO and oroxylin A, revealing specific interaction patterns and key residues crucial to the formation of the QDO-oroxylin A complex. Molecular docking simulations revealed a favorable binding affinity docking score: -5.6 kcalmol between Oroxylin A and the active site cavity of QDO, which was supported by Oroxylin As specific orientation Pose 3. Despite an observed RMSD value of 2.776 indicating a moderate deviation between the docked pose and the reference structure, the formation of two hydrogen bonds with GLN 93 chain D underscores specific molecular interactions driving the binding process. This hydrogen bond formation suggested the presence of a stable and specific binding mode between Oroxylin A and QDO, likely influencing the functional dynamics of the enzyme, necessitating further refinement and validation of the docking model. The ensuing deliberation on the implications of Oroxylin A include its potential as a modulator of QDO activity, emphasizing the importance of molecular-level insights in comprehending enzyme-compound interactions. Oroxylin A, a quercetin 2,3-dioxygenase inhibitor, was used in combination with other agents to prolong the biological impacts of quercetin, thereby amplifying its antioxidant and anti-inflammatory effects. This strategic approach exhibits promise in augmenting cardioprotective benefits, immune system support, and protection against diverse pathological conditions. Subsequent considerations of dosage, bioavailability, and healthcare professional consultation are imperative for judicious supplementation, particularly in individuals with prevailing health conditions or medications. This ongoing in silico study is dedicated to revealing the potential synergistic interactions of Oroxylin A, potentiating the long-term effects of quercetin and advancing our understanding of these intricacies.

 Elucidating the intricate interplay between enzymes and natural compounds is essential for designing therapeutic strategies. This study employs advanced computational techniques to explore the binding mechanisms between quercetin 2,3-dioxygenase QDO and oroxylin A, revealing specific interaction patterns and key residues crucial to the formation of the QDO-oroxylin A complex. Molecular docking simulations revealed a favorable binding affinity docking score: -5.6 kcalmol between Oroxylin A and the active site cavity of QDO, which was supported by Oroxylin As specific orientation Pose 3. Despite an observed RMSD value of 2.776 indicating a moderate deviation between the docked pose and the reference structure, the formation of two hydrogen bonds with GLN 93 chain D underscores specific molecular interactions driving the binding process. This hydrogen bond formation suggested the presence of a stable and specific binding mode between Oroxylin A and QDO, likely influencing the functional dynamics of the enzyme, necessitating further refinement and validation of the docking model. The ensuing deliberation on the implications of Oroxylin A include its potential as a modulator of QDO activity, emphasizing the importance of molecular-level insights in comprehending enzyme-compound interactions. Oroxylin A, a quercetin 2,3-dioxygenase inhibitor, was used in combination with other agents to prolong the biological impacts of quercetin, thereby amplifying its antioxidant and anti-inflammatory effects. This strategic approach exhibits promise in augmenting cardioprotective benefits, immune system support, and protection against diverse pathological conditions. Subsequent considerations of dosage, bioavailability, and healthcare professional consultation are imperative for judicious supplementation, particularly in individuals with prevailing health conditions or medications. This ongoing in silico study is dedicated to revealing the potential synergistic interactions of Oroxylin A, potentiating the long-term effects of quercetin and advancing our understanding of these intricacies.

 Elucidating the intricate interplay between enzymes and natural compounds is essential for designing therapeutic strategies. This study employs advanced computational techniques to explore the binding mechanisms between quercetin 2,3-dioxygenase QDO and oroxylin A, revealing specific interaction patterns and key residues crucial to the formation of the QDO-oroxylin A complex. Molecular docking simulations revealed a favorable binding affinity docking score: -5.6 kcalmol between Oroxylin A and the active site cavity of QDO, which was supported by Oroxylin As specific orientation Pose 3. Despite an observed RMSD value of 2.776 indicating a moderate deviation between the docked pose and the reference structure, the formation of two hydrogen bonds with GLN 93 chain D underscores specific molecular interactions driving the binding process. This hydrogen bond formation suggested the presence of a stable and specific binding mode between Oroxylin A and QDO, likely influencing the functional dynamics of the enzyme, necessitating further refinement and validation of the docking model. The ensuing deliberation on the implications of Oroxylin A include its potential as a modulator of QDO activity, emphasizing the importance of molecular-level insights in comprehending enzyme-compound interactions. Oroxylin A, a quercetin 2,3-dioxygenase inhibitor, was used in combination with other agents to prolong the biological impacts of quercetin, thereby amplifying its antioxidant and anti-inflammatory effects. This strategic approach exhibits promise in augmenting cardioprotective benefits, immune system support, and protection against diverse pathological conditions. Subsequent considerations of dosage, bioavailability, and healthcare professional consultation are imperative for judicious supplementation, particularly in individuals with prevailing health conditions or medications. This ongoing in silico study is dedicated to revealing the potential synergistic interactions of Oroxylin A, potentiating the long-term effects of quercetin and advancing our understanding of these intricacies.

Makale detayları

In Silico Elucidation of the Binding Mechanisms and Molecular Dynamics of Oroxylin A -2,3-Dioxygenase Interaction: An Insight into Therapeutic Potentiation of Quercetin’s Cardioprotection.

Yazarlar:

Azizeh Shadidizaji | Kağan Tolga Cinisli | Mohamad Warda | Öznur Altunlu | Sahar Memarkashani | Farideh Ghalamfarsa | Abdullah Menzek | Dilanur Ateş

Yayıncı:

Ataturk University

Ana Başlıklar:

Biological Psychology (Other)

Dergi:

Recent Trends in Pharmacology Vol.2 Issue 1, pp.27-35

Belge Tipi:

Makale

Yayın Tarihi:

3/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001317055

pISSN:

2980-194X

Quercetin

Quercetin 2

3-dioxygenase (QDO)

Oroxylin A

Molecular docking

Antioxidant

Cardioprotection.

Sayı

Makale detayları

Yazarlar: Azizeh Shadidizaji | Kağan Tolga Cinisli | Mohamad Warda | Öznur Altunlu | Sahar Memarkashani | Farideh Ghalamfarsa | Abdullah Menzek | Dilanur Ateş

Yayıncı: Ataturk University

Ana Başlıklar: Biological Psychology (Other)

Dergi: Recent Trends in Pharmacology Vol.2 Issue 1, pp.27-35

Belge Tipi: Makale

Yayın Tarihi: 3/2024

Belge Dili: İngilizce

Document ID (Org No.): 2001317055

pISSN: 2980-194X

Sayı

Yazarlar:

Azizeh Shadidizaji | Kağan Tolga Cinisli | Mohamad Warda | Öznur Altunlu | Sahar Memarkashani | Farideh Ghalamfarsa | Abdullah Menzek | Dilanur Ateş

Yayıncı:

Ataturk University

Ana Başlıklar:

Biological Psychology (Other)

Dergi:

Recent Trends in Pharmacology Vol.2 Issue 1, pp.27-35

Belge Tipi:

Makale

Yayın Tarihi:

3/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001317055

pISSN:

2980-194X