{"title":"Characterization of dovitinib–human serum albumin association potential through optical spectroscopic and in silico approaches","authors":"Cem Erkmen , Fazal Rehman , Saharuddin B. Mohamad","doi":"10.1016/j.saa.2025.126602","DOIUrl":null,"url":null,"abstract":"<div><div>The multitargeted receptor tyrosine kinase inhibitor, dovitinib (DTB) is reported to have a broad variety of pharmacological properties, which can be potentially useful in the treatment of various cancer entities. Association of DTB with the carrier protein, human serum albumin (HSA) was explored <em>via</em> experimental and <em>in silico</em> techniques. The reduction results of HSA fluorescence along with the hyperchromic effect in HSA's absorption signal observed with added DTB affirmed the DTB-HSA complex formation. Association of static quenching process for the complex was anticipated, while stabilization of the complex was asserted by a moderate binding affinity. The DTB–HSA complexation was expected to be maintained by hydrogen bonds, van der Waals and hydrophobic contacts. Variations in the protein (secondary and tertiary) conformations upon presence of DTB were verified from circular dichroism and Fourier transform infrared spectral results. Three-dimensional and synchronous fluorescence signals displayed variations in the microenvironmental make-up near protein fluorophores, consequent to the complex formation. Binding place of DTB, as detected by ligand displacement and molecular docking analyses, was found at Sudlow's site I in HSA. The results of the molecular dynamics simulations indicated that the DTB–HSA complex was stable.</div></div>","PeriodicalId":433,"journal":{"name":"Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy","volume":"343 ","pages":"Article 126602"},"PeriodicalIF":4.6000,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1386142525009096","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"SPECTROSCOPY","Score":null,"Total":0}
引用次数: 0
Abstract
The multitargeted receptor tyrosine kinase inhibitor, dovitinib (DTB) is reported to have a broad variety of pharmacological properties, which can be potentially useful in the treatment of various cancer entities. Association of DTB with the carrier protein, human serum albumin (HSA) was explored via experimental and in silico techniques. The reduction results of HSA fluorescence along with the hyperchromic effect in HSA's absorption signal observed with added DTB affirmed the DTB-HSA complex formation. Association of static quenching process for the complex was anticipated, while stabilization of the complex was asserted by a moderate binding affinity. The DTB–HSA complexation was expected to be maintained by hydrogen bonds, van der Waals and hydrophobic contacts. Variations in the protein (secondary and tertiary) conformations upon presence of DTB were verified from circular dichroism and Fourier transform infrared spectral results. Three-dimensional and synchronous fluorescence signals displayed variations in the microenvironmental make-up near protein fluorophores, consequent to the complex formation. Binding place of DTB, as detected by ligand displacement and molecular docking analyses, was found at Sudlow's site I in HSA. The results of the molecular dynamics simulations indicated that the DTB–HSA complex was stable.
期刊介绍:
Spectrochimica Acta, Part A: Molecular and Biomolecular Spectroscopy (SAA) is an interdisciplinary journal which spans from basic to applied aspects of optical spectroscopy in chemistry, medicine, biology, and materials science.
The journal publishes original scientific papers that feature high-quality spectroscopic data and analysis. From the broad range of optical spectroscopies, the emphasis is on electronic, vibrational or rotational spectra of molecules, rather than on spectroscopy based on magnetic moments.
Criteria for publication in SAA are novelty, uniqueness, and outstanding quality. Routine applications of spectroscopic techniques and computational methods are not appropriate.
Topics of particular interest of Spectrochimica Acta Part A include, but are not limited to:
Spectroscopy and dynamics of bioanalytical, biomedical, environmental, and atmospheric sciences,
Novel experimental techniques or instrumentation for molecular spectroscopy,
Novel theoretical and computational methods,
Novel applications in photochemistry and photobiology,
Novel interpretational approaches as well as advances in data analysis based on electronic or vibrational spectroscopy.