Biophysical and thermodynamical insights into the interaction of mefenamic acid with human serum albumin, based on combined multi-spectroscopic and molecular modeling approaches

Somaieh Soltani

Makale detayları

Biophysical and thermodynamical insights into the interaction of mefenamic acid with human serum albumin, based on combined multi-spectroscopic and molecular modeling approaches

Yazarlar:

Somaieh Soltani

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmacology and Pharmaceutical Sciences (Other)

Dergi:

Journal of Research in Pharmacy Vol.28 Issue 1, pp.372-384

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001346004

pISSN:

2630-6344

Anahtar kelimeler:

Özet:

 The molecular mechanism of interaction between Mefenamic acid MA and human serum albumin HSA was investigated. UV-Visible absorption, fluorescence, and FT-IR spectroscopies, with molecular docking, have been used for assay of complex formation, quenching mechanism study, thermodynamic evaluations, and molecular details of the interaction mechanism. The quenching constant Ksv of 1.51105 M-1 was obtained, while the results are indicating the dynamic quenching mechanism. The number of binding sites n and apparent binding constants KA were 1.51 and 6.55107 M-1, respectively that resembles positive cooperativity and and strong binding of MA to HSA. The negative sign of standard enthalpy change ΔH  -88.51 KJmol, standard entropy change ΔS  -146.24 Jmol K, and Gibbs free energy ΔG  -44.93 KJmol indicated that the van der Waals interactions and hydrogen bonds are facilitating the MA-HSA complex formation. Addition of the metal ions, glucose, urea, and basic pHs decrease the MA-HSA binding constant. Molecular docking simulation showed that mainly positively charged amino acid residues contribute to the MA-HSA interaction.

 The molecular mechanism of interaction between Mefenamic acid MA and human serum albumin HSA was investigated. UV-Visible absorption, fluorescence, and FT-IR spectroscopies, with molecular docking, have been used for assay of complex formation, quenching mechanism study, thermodynamic evaluations, and molecular details of the interaction mechanism. The quenching constant Ksv of 1.51105 M-1 was obtained, while the results are indicating the dynamic quenching mechanism. The number of binding sites n and apparent binding constants KA were 1.51 and 6.55107 M-1, respectively that resembles positive cooperativity and and strong binding of MA to HSA. The negative sign of standard enthalpy change ΔH  -88.51 KJmol, standard entropy change ΔS  -146.24 Jmol K, and Gibbs free energy ΔG  -44.93 KJmol indicated that the van der Waals interactions and hydrogen bonds are facilitating the MA-HSA complex formation. Addition of the metal ions, glucose, urea, and basic pHs decrease the MA-HSA binding constant. Molecular docking simulation showed that mainly positively charged amino acid residues contribute to the MA-HSA interaction.

 The molecular mechanism of interaction between Mefenamic acid MA and human serum albumin HSA was investigated. UV-Visible absorption, fluorescence, and FT-IR spectroscopies, with molecular docking, have been used for assay of complex formation, quenching mechanism study, thermodynamic evaluations, and molecular details of the interaction mechanism. The quenching constant Ksv of 1.51105 M-1 was obtained, while the results are indicating the dynamic quenching mechanism. The number of binding sites n and apparent binding constants KA were 1.51 and 6.55107 M-1, respectively that resembles positive cooperativity and and strong binding of MA to HSA. The negative sign of standard enthalpy change ΔH  -88.51 KJmol, standard entropy change ΔS  -146.24 Jmol K, and Gibbs free energy ΔG  -44.93 KJmol indicated that the van der Waals interactions and hydrogen bonds are facilitating the MA-HSA complex formation. Addition of the metal ions, glucose, urea, and basic pHs decrease the MA-HSA binding constant. Molecular docking simulation showed that mainly positively charged amino acid residues contribute to the MA-HSA interaction.

 The molecular mechanism of interaction between Mefenamic acid MA and human serum albumin HSA was investigated. UV-Visible absorption, fluorescence, and FT-IR spectroscopies, with molecular docking, have been used for assay of complex formation, quenching mechanism study, thermodynamic evaluations, and molecular details of the interaction mechanism. The quenching constant Ksv of 1.51105 M-1 was obtained, while the results are indicating the dynamic quenching mechanism. The number of binding sites n and apparent binding constants KA were 1.51 and 6.55107 M-1, respectively that resembles positive cooperativity and and strong binding of MA to HSA. The negative sign of standard enthalpy change ΔH  -88.51 KJmol, standard entropy change ΔS  -146.24 Jmol K, and Gibbs free energy ΔG  -44.93 KJmol indicated that the van der Waals interactions and hydrogen bonds are facilitating the MA-HSA complex formation. Addition of the metal ions, glucose, urea, and basic pHs decrease the MA-HSA binding constant. Molecular docking simulation showed that mainly positively charged amino acid residues contribute to the MA-HSA interaction.

Makale detayları

Biophysical and thermodynamical insights into the interaction of mefenamic acid with human serum albumin, based on combined multi-spectroscopic and molecular modeling approaches

Yazarlar:

Somaieh Soltani

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmacology and Pharmaceutical Sciences (Other)

Dergi:

Journal of Research in Pharmacy Vol.28 Issue 1, pp.372-384

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001346004

pISSN:

2630-6344

Mefenamic acid

NSAID-HSA interaction

Spectroscopy methods

Molecular docking

Sayı

Makale detayları

Biophysical and thermodynamical insights into the interaction of mefenamic acid with human serum albumin, based on combined multi-spectroscopic and molecular modeling approaches

Yazarlar: Somaieh Soltani

Yayıncı: Marmara University

Ana Başlıklar: Pharmacology and Pharmaceutical Sciences (Other)

Dergi: Journal of Research in Pharmacy Vol.28 Issue 1, pp.372-384

Belge Tipi: Makale

Yayın Tarihi: 6/2025

Belge Dili: İngilizce

Document ID (Org No.): 2001346004

pISSN: 2630-6344

Mefenamic acid

NSAID-HSA interaction

Spectroscopy methods

Molecular docking

Sayı

Yazarlar:

Somaieh Soltani

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmacology and Pharmaceutical Sciences (Other)

Dergi:

Journal of Research in Pharmacy Vol.28 Issue 1, pp.372-384

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001346004

pISSN:

2630-6344