Investigation of the letrozole interaction with human serum albumin using a combination of MCR-ALS chemometrics, multi-spectrometric and molecular modeling

Somaieh Soltani

Article Details

Investigation of the letrozole interaction with human serum albumin using a combination of MCR-ALS chemometrics, multi-spectrometric and molecular modeling

Authors:

Somaieh Soltani

Publisher:

Marmara University

Main Topics:

Pharmacology and Pharmaceutical Sciences (Other)

Journal:

Journal of Research in Pharmacy Vol.28 Issue 1, pp.1-15

Document Type:

Article

Publication Date:

6/2025

Document Language:

English

Document ID (Org No.):

2001345977

pISSN:

2630-6344

Keywords:

Abstract:

 Letrozole-HSA human serum albumin binding was studied using various spectroscopic techniques, MCR-ALS multivariate curve resolution alternating least squares chemometrics method, and molecular modelings. Binding constant at different temperatures, main interacted sites properties, thermodynamic parameters, HSA conformation in complex form was obtained using the relevant data. Due to the fluorescence emission wavelength overlap of LET and HSA, fluorescence emission enhancement was seen at the emission wavelength of 340 nm, following the excitation at 278 nm rather than fluorescence quenching. MCR-ALS analysis of UV-Vis absorption and fluorescence emission data approved the complex formation between LET and HSA. The fluorescence emission quenching was observed at 320 nm rather than 340 nm. The emission data were fitted to the Stern-Volmer, vant Hoff, and Hill models to calculate the quenching and binding constants. The results showed that LET binds to HSA with a binding constant of 2.25  104 M-1 that resembles the moderate binding capacity of LET to HSA. Furthermore, decreased biding constant at higher temperatures and decreased quenching constants at higher temperatures showed static quenching constant. Thermodynamic analysis and simultaneous competitive binding studies showed that LET interacts with HSAs subdomain IIA and IIIA mainly by hydrogen and Van der Waals bonds. The results agree with molecular modeling studies. FTIR and circular dichroism CD results revealed the reduced alpha-helical structure of HSA in LET-HSA complex compared to non-bound form.

 Letrozole-HSA human serum albumin binding was studied using various spectroscopic techniques, MCR-ALS multivariate curve resolution alternating least squares chemometrics method, and molecular modelings. Binding constant at different temperatures, main interacted sites properties, thermodynamic parameters, HSA conformation in complex form was obtained using the relevant data. Due to the fluorescence emission wavelength overlap of LET and HSA, fluorescence emission enhancement was seen at the emission wavelength of 340 nm, following the excitation at 278 nm rather than fluorescence quenching. MCR-ALS analysis of UV-Vis absorption and fluorescence emission data approved the complex formation between LET and HSA. The fluorescence emission quenching was observed at 320 nm rather than 340 nm. The emission data were fitted to the Stern-Volmer, vant Hoff, and Hill models to calculate the quenching and binding constants. The results showed that LET binds to HSA with a binding constant of 2.25  104 M-1 that resembles the moderate binding capacity of LET to HSA. Furthermore, decreased biding constant at higher temperatures and decreased quenching constants at higher temperatures showed static quenching constant. Thermodynamic analysis and simultaneous competitive binding studies showed that LET interacts with HSAs subdomain IIA and IIIA mainly by hydrogen and Van der Waals bonds. The results agree with molecular modeling studies. FTIR and circular dichroism CD results revealed the reduced alpha-helical structure of HSA in LET-HSA complex compared to non-bound form.

 Letrozole-HSA human serum albumin binding was studied using various spectroscopic techniques, MCR-ALS multivariate curve resolution alternating least squares chemometrics method, and molecular modelings. Binding constant at different temperatures, main interacted sites properties, thermodynamic parameters, HSA conformation in complex form was obtained using the relevant data. Due to the fluorescence emission wavelength overlap of LET and HSA, fluorescence emission enhancement was seen at the emission wavelength of 340 nm, following the excitation at 278 nm rather than fluorescence quenching. MCR-ALS analysis of UV-Vis absorption and fluorescence emission data approved the complex formation between LET and HSA. The fluorescence emission quenching was observed at 320 nm rather than 340 nm. The emission data were fitted to the Stern-Volmer, vant Hoff, and Hill models to calculate the quenching and binding constants. The results showed that LET binds to HSA with a binding constant of 2.25  104 M-1 that resembles the moderate binding capacity of LET to HSA. Furthermore, decreased biding constant at higher temperatures and decreased quenching constants at higher temperatures showed static quenching constant. Thermodynamic analysis and simultaneous competitive binding studies showed that LET interacts with HSAs subdomain IIA and IIIA mainly by hydrogen and Van der Waals bonds. The results agree with molecular modeling studies. FTIR and circular dichroism CD results revealed the reduced alpha-helical structure of HSA in LET-HSA complex compared to non-bound form.

 Letrozole-HSA human serum albumin binding was studied using various spectroscopic techniques, MCR-ALS multivariate curve resolution alternating least squares chemometrics method, and molecular modelings. Binding constant at different temperatures, main interacted sites properties, thermodynamic parameters, HSA conformation in complex form was obtained using the relevant data. Due to the fluorescence emission wavelength overlap of LET and HSA, fluorescence emission enhancement was seen at the emission wavelength of 340 nm, following the excitation at 278 nm rather than fluorescence quenching. MCR-ALS analysis of UV-Vis absorption and fluorescence emission data approved the complex formation between LET and HSA. The fluorescence emission quenching was observed at 320 nm rather than 340 nm. The emission data were fitted to the Stern-Volmer, vant Hoff, and Hill models to calculate the quenching and binding constants. The results showed that LET binds to HSA with a binding constant of 2.25  104 M-1 that resembles the moderate binding capacity of LET to HSA. Furthermore, decreased biding constant at higher temperatures and decreased quenching constants at higher temperatures showed static quenching constant. Thermodynamic analysis and simultaneous competitive binding studies showed that LET interacts with HSAs subdomain IIA and IIIA mainly by hydrogen and Van der Waals bonds. The results agree with molecular modeling studies. FTIR and circular dichroism CD results revealed the reduced alpha-helical structure of HSA in LET-HSA complex compared to non-bound form.

Article Details

Investigation of the letrozole interaction with human serum albumin using a combination of MCR-ALS chemometrics, multi-spectrometric and molecular modeling

Authors:

Somaieh Soltani

Publisher:

Marmara University

Main Topics:

Pharmacology and Pharmaceutical Sciences (Other)

Journal:

Journal of Research in Pharmacy Vol.28 Issue 1, pp.1-15

Document Type:

Article

Publication Date:

6/2025

Document Language:

English

Document ID (Org No.):

2001345977

pISSN:

2630-6344

Letrozole

Human serum albumin

spectroscopy

MCR-ALS

Emission spectra overlap

Issues

Article Details

Investigation of the letrozole interaction with human serum albumin using a combination of MCR-ALS chemometrics, multi-spectrometric and molecular modeling

Authors: Somaieh Soltani

Publisher: Marmara University

Main Topics: Pharmacology and Pharmaceutical Sciences (Other)

Journal: Journal of Research in Pharmacy Vol.28 Issue 1, pp.1-15

Document Type: Article

Publication Date: 6/2025

Document Language: English

Document ID (Org No.): 2001345977

pISSN: 2630-6344

Letrozole

Human serum albumin

spectroscopy

MCR-ALS

Emission spectra overlap

Issues

Authors:

Somaieh Soltani

Publisher:

Marmara University

Main Topics:

Pharmacology and Pharmaceutical Sciences (Other)

Journal:

Journal of Research in Pharmacy Vol.28 Issue 1, pp.1-15

Document Type:

Article

Publication Date:

6/2025

Document Language:

English

Document ID (Org No.):

2001345977

pISSN:

2630-6344