Multiple Spectroscopic, Docking and Cytotoxic Study of a Synthesized 2,2′ Bipyridin Phenyl Isopentylglycin Pt(II) Nitrate Complex: Human Serum Albumin and Breast Cancer Cell Line of MDA-MB231 as Targets

Nourizadeh, Sara; Divsalar, Adeleh; Fekri, M.; Ghalandari, Behafarid; Eslami-Moghadam, Mahbubeh; Saboury, Ali Akbar; Abbasi, Saba

doi:10.1007/s10895-018-2216-5

Cited by 6 publications

(5 citation statements)

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“…The molecular docking studies are useful in exploring the details related to interaction and the binding sites of a ligand on protein and binding energies of small molecules with proteins . Therefore, the results of HEX 8.0 calculations illustrated hydrophobic interactions between drug site I and II of HSA and the 2(C 12 Cys) GS (Figure ).…”

Section: Resultsmentioning

confidence: 99%

Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study

et al. 2019

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Binding effect and interaction of N,N′-dialkyl cystine based gemini surfactant (GS); 2(C12Cys) with human serum albumin (HSA) were systematically investigated by the techniques such as surface tension measurement, UV−visible spectroscopy, fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular docking studies. The surface tension measurement exhibited that HSA shifted the critical micelle concentration of the 2(C12Cys) GS to the higher side that confirms the complex formation among 2(C12Cys) GS and HSA which was also verified by UV–visible, fluorescence, and CD spectroscopy. Increase in the concentration of 2(C12Cys) GS increases the absorption of the HSA protein but has a reverse effect on the fluorescence intensity. The analysis of UV–visible study with the help of a static quenching method showed that the value acquired for the bimolecular quenching constant (kq) quenches the intrinsic fluorescence of the HSA protein. Synchronous fluorescence spectrometry declared that the induced-binding conformational changes in HSA and CD results explained the variations in the secondary arrangement of the protein in presence of 2(C12Cys) GS. The present study revealed that the interaction between 2(C12Cys) GS and HSA is important for the preparation and properties of medicines. Molecular docking study provides insight into the specific binding site of 2(C12Cys) GS into the sites of HSA.

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Section: Resultsmentioning

confidence: 99%

Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study

et al. 2019

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“…Serum albumin (SA), the most abundant protein in mammalian blood plasma, is the principal transporter of various solutes within plasma [175][176][177]. Generally, SA responds to pH and temperature changes, is soluble at high concentrations, and gels quickly under certain circumstances [178,179].…”

Section: Serum Albumin-based Hydrogelsmentioning

confidence: 99%

Protein-Based Hydrogels: Promising Materials for Tissue Engineering

et al. 2022

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The successful design of a hydrogel for tissue engineering requires a profound understanding of its constituents’ structural and molecular properties, as well as the proper selection of components. If the engineered processes are in line with the procedures that natural materials undergo to achieve the best network structure necessary for the formation of the hydrogel with desired properties, the failure rate of tissue engineering projects will be significantly reduced. In this review, we examine the behavior of proteins as an essential and effective component of hydrogels, and describe the factors that can enhance the protein-based hydrogels’ structure. Furthermore, we outline the fabrication route of protein-based hydrogels from protein microstructure and the selection of appropriate materials according to recent research to growth factors, crucial members of the protein family, and their delivery approaches. Finally, the unmet needs and current challenges in developing the ideal biomaterials for protein-based hydrogels are discussed, and emerging strategies in this area are highlighted.

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“…The sensitivity of Trp is along with changes in the emission intensity. Hence, the emission of Trp residue is mainly used for the intrinsic fluorescence measurements [40,41]. Hb contains six Trp residues.…”

Section: Palladium (Ii) Complexes-hb Interaction Studymentioning

confidence: 99%

“…3) was used as followed. F 0 /ΔF is linearly dependent on the quencher concentration [Q] −1 [41]. The results are shown in Fig.…”

Section: Palladium (Ii) Complexes-hb Interaction Studymentioning

confidence: 99%

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Protein interaction and in vitro cytotoxicity studies of newly designed palladium (II) nitrate complexes: spectrochemical, theoretical and biological assessments

et al. 2020

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The biological assessments of new synthesized palladium (II) complexes [1, 10-phenanthroline hexyl dithiocarbamato palladium (II) nitrate (complex I), and 1, 10-phenanthroline butyl dithiocarbamato palladium (II) nitrate (complex II)] were investigated using in vitro cytotoxicity and molecular interaction studies. The in vitro cytotoxicity studies were done against human cervical HeLa cancer cell line and human breast MDA-MB-468 cancer cell line. The interaction evaluations were done using human hemoglobin (Hb) as the primary target of novel palladium (II) complexes using spectroscopy methods of fluorescence and circular dichroism at various temperatures of 25, 37, 42, and 47 °C as well as molecular docking. The results have indicated complex I and complex II are quite similar in functionality. They induced apoptotic cell death so that they showed a significant growth inhibitory effect against HeLa and MDA-MB-468 cells. The fluorescence spectroscopy and molecular docking indicated that there is only one binding site for new palladium (II) complexes on Hb. The interaction studies revealed complex I and complex II have the same structural effects and similar binding properties on Hb. Finally, the results showed the newly synthesized palladium (II) complexes have no structural degradation on Hb. Therefore, they can be introduced as promising candidates in cancer treatment.

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Multiple Spectroscopic, Docking and Cytotoxic Study of a Synthesized 2,2′ Bipyridin Phenyl Isopentylglycin Pt(II) Nitrate Complex: Human Serum Albumin and Breast Cancer Cell Line of MDA-MB231 as Targets

Cited by 6 publications

References 43 publications

Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study

Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study

Protein-Based Hydrogels: Promising Materials for Tissue Engineering

Protein interaction and in vitro cytotoxicity studies of newly designed palladium (II) nitrate complexes: spectrochemical, theoretical and biological assessments

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