Characterization of the binding of an anticancer drug, lapatinib to human serum albumin

Kabir, Md. Zahirul; Mukarram, Abdul Kadir; Mohamad, Saharuddin Bin; Alias, Zazali; Tayyab, Saad

doi:10.1016/j.jphotobiol.2016.04.005

Cited by 43 publications

(16 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Both the Ksv and K revealed that the interaction of Iro with HSA was weak; much lower than other drugs e.g. lapatinib, 5-fluorouracil and captopril (Gao et al, 2011;Kabir et al, 2016;Sun et al, 2012a). Verily, this also is in consonance with an earlier study, which has reported other proteins to have interacted more with Iro than HSA in a magnetic nanoparticle system (Tamyurek et al, 2015).…”

Section: Fluorescence Quenchingsupporting

confidence: 85%

Rational design of polysorbate 80 stabilized human serum albumin nanoparticles tailored for high drug loading and entrapment of irinotecan

Taneja

Singh

2018

International Journal of Pharmaceutics

View full text Add to dashboard Cite

Human serum albumin (HSA) nanoparticles are considered to be versatile carrier of anticancer agents in efficiently delivering the drug to the tumor site without causing any toxicity. The aim of the study was to develop stable HSA nanoparticles (NPs) of drug irinotecan (Iro) having slightly water solubility and moderate HSA binding. A novel strategy of employing a hydrophilic non-ionic surfactant polysorbate 80 which forms protein-polysorbate 80 complex with increased affinity and improvement in Iro-HSA binding has been used to maximize the loading and entrapment efficiency of Iro in HSA-NPs. Bespoke nanoparticles with entrapment efficiency (79.09%) and drug loading of 9.62% could be achieved with spherical shape and particle size of 77.38 nm, 0.290 polydispersity index and -23.7 mv Zeta potential. The drug entrapment in nanoparticles was confirmed by Differential Scanning Calorimeter, Fourier Transformation Infrared Spectroscopy and Fluorescence Spectroscopy. In vitro release of Iro from NPs showed biphasic-release with initial burst followed by prolonged release upto 24 h. The short-term stability investigation of nanodispersion showed no significant changes in physicochemical properties of NPs. Long-term studies on freeze dried Iro-HSA-NPs indicated good stability of NPs up to 12 months. This is the first report for efficient fabrication of Iro delivery system based on HSA nanoparticles.

show abstract

Section: Fluorescence Quenchingsupporting

confidence: 85%

Rational design of polysorbate 80 stabilized human serum albumin nanoparticles tailored for high drug loading and entrapment of irinotecan

Taneja

Singh

2018

International Journal of Pharmaceutics

View full text Add to dashboard Cite

show abstract

“…Our previous work revealed that other ACE inhibitors were capable to bind to BSA with association constants in the order of 10 4 M −1 , which was higher than that of fosinopril . Moreover, a progressive decrease in the K b value with the increasing temperature signified lower stability of the fosinopril‐BSA complex at higher temperature …”

Section: Resultsmentioning

confidence: 93%

“…The interaction forces involved in the fosinopril‐BSA complex formation can be obtained from the thermodynamic data, ie, enthalpy change (Δ H 0 ), entropy change (Δ S 0 ), and Gibbs free energy change (Δ G 0 ). A negative sign of Δ G 0 determines the feasibility of the binding reaction between small molecules and proteins, the signs and magnitudes of Δ H 0 and Δ S 0 provide an insight into the forces involved in the complex formation . In the case of a small molecule binding to a protein, these may include hydrogen bonds, van der Waals, electrostatic, and hydrophobic interactions .…”

Section: Resultsmentioning

confidence: 99%

“…[10][11][12][13] Moreover, a progressive decrease in the K b value with the increasing temperature signified lower stability of the fosinopril-BSA complex at higher temperature. 28 The interaction forces involved in the fosinopril-BSA complex formation can be obtained from the thermodynamic data, ie, enthalpy change (ΔH 0 ), entropy change (ΔS 0 ), and Gibbs free energy change (ΔG 0 ). A negative sign of ΔG 0 determines the feasibility of the binding reaction between small molecules and proteins, the signs and magnitudes of ΔH 0 and ΔS 0 provide an insight into the forces involved in the complex formation.…”

Section: Binding and Thermodynamic Characteristics Of Interactionsmentioning

confidence: 99%

“…A negative sign of ΔG 0 determines the feasibility of the binding reaction between small molecules and proteins, the signs and magnitudes of ΔH 0 and ΔS 0 provide an insight into the forces involved in the complex formation. 28 In the case of a small molecule binding to a protein, these may include hydrogen bonds, van der Waals, electrostatic, and hydrophobic interactions. 29 To elucidate the interaction of fosinopril with BSA, the thermodynamic parameters were calculated from van't Hoff (Equation S3) and thermodynamic equations (Equation S4).…”

Section: Binding and Thermodynamic Characteristics Of Interactionsmentioning

confidence: 99%

See 2 more Smart Citations

Intermolecular interaction of fosinopril with bovine serum albumin (BSA): The multi‐spectroscopic and computational investigation

Zhou

Pan

Lou

et al. 2018

J of Molecular Recognition

View full text Add to dashboard Cite

The intermolecular interaction of fosinopril, an angiotensin converting enzyme inhibitor with bovine serum albumin (BSA), has been investigated in physiological buffer (pH 7.4) by multi-spectroscopic methods and molecular docking technique. The results obtained from fluorescence and UV absorption spectroscopy revealed that the fluorescence quenching mechanism of BSA induced by fosinopril was mediated by the combined dynamic and static quenching, and the static quenching was dominant in this system. The binding constant, K , value was found to lie between 2.69 × 10 and 9.55 × 10 M at experimental temperatures (293, 298, 303, and 308 K), implying the low or intermediate binding affinity between fosinopril and BSA. Competitive binding experiments with site markers (phenylbutazone and diazepam) suggested that fosinopril preferentially bound to the site I in sub-domain IIA on BSA, as evidenced by molecular docking analysis. The negative sign for enthalpy change (ΔH ) and entropy change (ΔS ) indicated that van der Waals force and hydrogen bonds played important roles in the fosinopril-BSA interaction, and 8-anilino-1-naphthalenesulfonate binding assay experiments offered evidence of the involvements of hydrophobic interactions. Moreover, spectroscopic results (synchronous fluorescence, 3-dimensional fluorescence, and Fourier transform infrared spectroscopy) indicated a slight conformational change in BSA upon fosinopril interaction.

show abstract

Characterization of Locally Excited and Charge‐Transfer States of the Anticancer Drug Lapatinib by Ultrafast Spectroscopy and Computational Studies

Vayá

Andreu

Lence

et al. 2020

Chemistry A European J

View full text Add to dashboard Cite

Lapatinib (LAP) is an anticancer drug, which is metabolized to the N-a nd O-dealkylated products (N-LAP and O-LAP,r espectively). In view of the photosensitizing potential of relatedd rugs, ac omplete experimentala nd theoretical study has been performedo nL AP, N-LAP and O-LAP, both in solution and upon complexationw ith human serum albumin (HSA). In organic solvents, coplanar locally excited (LE) emissive states are generated;t hey rapidly evolve towards twisted intramolecularc harge-transfer (ICT) states. By contrast, within HSA only LE states are detected. Accordingly,f emtosecond transient absorption reveals av ery fast switching (ca. 2ps) from LE (l max = 550 nm) to ICT states (l max = 480 nm) in solution, whereas within HSA the LE species become stabilized and live much longer(up to the ns scale). Interestingly,m olecular dynamics simulation studies confirm that the coplanar orientation is preferred for LAP (or to al esser extent N-LAP) within HSA, explaining the experimental results.

show abstract

Characterization of the binding of an anticancer drug, lapatinib to human serum albumin

Cited by 43 publications

References 51 publications

Rational design of polysorbate 80 stabilized human serum albumin nanoparticles tailored for high drug loading and entrapment of irinotecan

Rational design of polysorbate 80 stabilized human serum albumin nanoparticles tailored for high drug loading and entrapment of irinotecan

Intermolecular interaction of fosinopril with bovine serum albumin (BSA): The multi‐spectroscopic and computational investigation

Characterization of Locally Excited and Charge‐Transfer States of the Anticancer Drug Lapatinib by Ultrafast Spectroscopy and Computational Studies

Contact Info

Product

Resources

About