A Thermodynamic Study on the Binding of Human Serum Albumin with Lanthanum Ion

Behbehani, G. Rezaei; Divsalar, Adeleh; Saboury, Ali Akbar; Faridbod, Farnoush

doi:10.1002/cjoc.201090047

Cited by 6 publications

(4 citation statements)

References 29 publications

(13 reference statements)

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“…Exploring the binding of proteins to drugs can provide valuable insights into the structural aspects that determine the therapeutic effects of the drugs. Consequently, the investigation of these interactions has become a crucial field of study in clinical medicine, chemistry, and life science ( Rezaei Behbehani et al, 2010 ; Zhang et al, 2010 ; Wu et al, 2011 ; Alfi et al, 2017 ; Asadi et al, 2017 ; Cao et al, 2022 ; Cao et al, 2023 ). In most cases, drugs travel through the bloodstream and reach their target tissues by interacting with serum albumin, which is the plentiful protein in the circulatory framework.…”

Section: Introductionmentioning

confidence: 99%

RETRACTED: In vitro BSA-binding, antimicrobial, and antitumor activity against human cancer cell lines of two lanthanide (III) complexes

et al. 2023

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The investigation involved examining the binding of two lanthanide complexes, specifically those containing Holmium (Ho) and Dysprosium (Dy), with a ligand called 1, 10-phenanthroline (phen), and bovine serum albumin (BSA). The evaluation was carried out utilizing fluorescence measurements, Förster theory, and docking studies. The findings indicated that both the Ho-complex and Dy-complex possessed a significant ability to quench the emission of the protein. Furthermore, the primary mechanism of interaction was identified as a static process. The Kb values indicate a strong tendency of these complexes for binding with BSA. The Kb values show the strangely high affinity of BSA to complexes and the following order for binding affinity: Ho-complex > Dy-complex. The thermodynamic parameters were found to be negative, affirming that the main forces driving the interaction between BSA and the lanthanide complexes are van der Waals engagement and hydrogen bonds. Additionally, the investigation included the examination of competition site markers, and molecular docking proposed that the engagement sites of the Ho-complex and Dy-complex with BSA were predominantly located in site 3 (specifically, subdomain IB). Moreover, the Ho-complex and Dy-complex were specifically chosen for their potential anticancer and antimicrobial properties. Consequently, these complexes could present promising prospects as novel candidates for anti-tumor and antibacterial applications.

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Section: Introductionmentioning

confidence: 99%

RETRACTED: In vitro BSA-binding, antimicrobial, and antitumor activity against human cancer cell lines of two lanthanide (III) complexes

et al. 2023

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“…We have shown previously that the heats of the ligand + HSA interactions in the aqueous solvent mixtures, can be calculated via the following equation [9][10][11][12][13][14]:…”

Section: Resultsmentioning

confidence: 99%

A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin

Behbehani

Sadr

Nabipur

et al. 2013

Journal of Chemistry

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Binding parameters of the N-phenyl benzene sulfonyl hydrazide, sulfonamide, and nanosulfonamide interaction with human serum albumin were determined by calorimetry method. The obtained binding parameters indicated that sulfonamide in the second binding sites has higher affinity for binding than the first binding sites. The binding process of sulfonamide to HSA is both enthalpy and entropy driven. The associated equilibrium constants confirm that sulfonamide binds to HSA with high affinity (2.2×106and 3.86105 M−1for first and second sets of binding sites, resp.). The obtained results indicate that sulfonamide increases the HSA antioxidant property. Nanosulfonamide has much more affinity for HSA (3.6×106 M−1) than sulfonamide.

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“…We have shown previously that the heats of the ligand ? JBU interactions in the aqueous solvent mixtures can be calculated via the following equation [7][8][9][10][11][12]:…”

Section: Resultsmentioning

confidence: 99%

The Interaction of Ferric Ions with Jack Bean Urease by Isothermal Titration Calorimetry

Behbehani

Barzegar

2013

Natl. Acad. Sci. Lett.

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The aim of the investigations was to measure the influence of Fe 3? ion on jack bean urease (JBU) activity. Interaction between Fe 3? and JBU, is examined using isothermal titration calorimetry. It was found that Fe 3? ions acted as a non-cooperative inhibitor of JBU, and there is a set of 12 identical and independent binding sites for Fe 3? ions. The small structural parameters show that there are little changes on the JBU structure, indicating that Fe 3? has minor effect on the JBU activity. The association equilibrium constant is 42,484.13 ± 110 mol l-1 , indicating the moderate interaction of Fe 3? ion with JBU. The molar enthalpy of binding is DH =-4.33 kJ mol-1 .

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A Thermodynamic Study on the Binding of Human Serum Albumin with Lanthanum Ion

Cited by 6 publications

References 29 publications

RETRACTED: In vitro BSA-binding, antimicrobial, and antitumor activity against human cancer cell lines of two lanthanide (III) complexes

RETRACTED: In vitro BSA-binding, antimicrobial, and antitumor activity against human cancer cell lines of two lanthanide (III) complexes

A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin

The Interaction of Ferric Ions with Jack Bean Urease by Isothermal Titration Calorimetry

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