Synthesis, tyrosinase inhibition and transportation behavior of novel β-enamino thiosemicarbazide derivatives by human serum albumin

Chaves, Otávio Augusto; Santos, Margareth Rose de Lima; Oliveira, Márcia C.C. de; Sant’Anna, Carlos Maurício R.; Ferreira, Romulo Correia; Echevarrı́a, Aurea; Netto‐Ferreira, José Carlos

doi:10.1016/j.molliq.2018.01.083

Cited by 45 publications

(17 citation statements)

References 55 publications

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“…The fluorescence decay for HSA is bi-exponential, with lifetimes of τ 1 = 1.73 ± 0.16 ns and τ 2 = 5.54 ± 0.12 ns ( Figure S8, Supplementary Material), which is in accordance with literature data [64,65]. Both fluorescence lifetimes are independent of the addition of any of the mesoionic compounds 5a-d (1.35 × 10 −5 M concentration) (Table 3), which is a clear indication of a static process as the main mechanism fluorescence quenching in the interaction between HSA and the mesoionic compounds under study [47]. Similar results have been reported previously for the interaction between HSA and piperonal mesoionic derivatives [66].…”

Section: Experimental Binding Abilitysupporting

confidence: 90%

“…Similar results have been reported previously for the interaction between HSA and piperonal mesoionic derivatives [66]. The modified Stern-Volmer binding constant (K a ) is related to the protein-ligand interaction, and its magnitude is important for understanding the distribution of a drug in the human bloodstream [47,61]. Moderate values for K a , in the order of 10 4 M −1 , at 296, 303, and 310 K, were obtained for the interaction HSA:5a-d ( Figure S9 in the Supplementary Material and Table 2), indicating the viability of the absorption and distribution of these mesoionic compounds to various tissues [46,48,61].…”

Section: Experimental Binding Abilitysupporting

confidence: 86%

“…The main fluorophore of HSA is the tryptophan (Trp-214) residue, which is located in a large hydrophobic cavity in subdomain IIA (site I) [45]. Therefore, the intrinsic fluorescence intensity of Trp-214 residue is a common phenomenon used to investigate the interaction of ligands with HSA [46][47][48].…”

Section: Introductionmentioning

confidence: 99%

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Synthetic (E)-3-Phenyl-5-(phenylamino)-2-styryl-1,3,4-thiadiazol-3-ium Chloride Derivatives as Promising Chemotherapy Agents on Cell Lines Infected with HTLV-1

et al. 2020

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Synthesis of four compounds belonging to mesoionic class, (E)-3-phenyl-5-(phenylamino)-2-styryl-1,3,4-thiadiazol-3-ium chloride derivatives (5a–d) and their biological evaluation against MT2 and C92 cell lines infected with human T-cell lymphotropic virus type-1 (HTLV-1), which causes adult T-cell leukemia/lymphoma (ATLL), and non-infected cell lines (Jurkat) are reported. The compounds were obtained by convergent synthesis under microwave irradiation and the cytotoxicity was evaluated using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assays. Results showed IC50 values of all compounds in the range of 1.51–7.70 μM in HTLV-1-infected and non-infected cells. Furthermore, it was observed that 5b could induce necrosis after 24 h for Jurkat and MT2 cell lines. The experimental (fluorimetric method) and theoretical (molecular docking) results suggested that the mechanism of action for 5b could be related to its capacity to intercalate into DNA. Moreover, the preliminary pharmacokinetic profile of the studied compounds (5a–d) was obtained through human serum albumin (HSA) binding affinity using multiple spectroscopic techniques (circular dichroism, steady-state and time-resolved fluorescence), zeta potential and molecular docking calculations. The interaction HSA:5a–d is spontaneous and moderate (Ka ~ 104 M−1) via a ground-state association, without significantly perturbing both the secondary and surface structures of the albumin in the subdomain IIA (site I), indicating feasible biodistribution in the human bloodstream.

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Section: Experimental Binding Abilitysupporting

confidence: 90%

Section: Experimental Binding Abilitysupporting

confidence: 86%

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Synthetic (E)-3-Phenyl-5-(phenylamino)-2-styryl-1,3,4-thiadiazol-3-ium Chloride Derivatives as Promising Chemotherapy Agents on Cell Lines Infected with HTLV-1

et al. 2020

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“…The steady-state fluorescence spectrum of HSA presented maximum fluorescence emission at 340 nm. Upon successive additions of RPF101 to HSA solution fluorescence quenching can be observed without any blue or red shift (Stokes’ shift), indicating that the ligand binding does not perturb significantly the fluorophore environment [ 21 , 22 ]. In order to confirm this result, synchronous fluorescence (SF) spectra was carried out at Δλ = 15 and 60 nm.…”

Section: Discussionmentioning

confidence: 99%

“…The figure of the best docking pose for each sample was generated by the PyMOL Delano Scientific LLC program. Further details can be found in previous publications [ 17 , 22 ].…”

Section: Methodsmentioning

confidence: 99%

Multi-Spectroscopic and Theoretical Analysis on the Interaction between Human Serum Albumin and a Capsaicin Derivative—RPF101

et al. 2018

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The interaction between the main carrier of endogenous and exogenous compounds in the human bloodstream (human serum albumin, HSA) and a potential anticancer compound (the capsaicin analogue RPF101) was investigated by spectroscopic techniques (circular dichroism, steady-state, time-resolved, and synchronous fluorescence), zeta potential, and computational method (molecular docking). Steady-state and time-resolved fluorescence experiments indicated an association in the ground state between HSA:RPF101. The interaction is moderate, spontaneous (ΔG° < 0), and entropically driven (ΔS° = 0.573 ± 0.069 kJ/molK). This association does not perturb significantly the potential surface of the protein, as well as the secondary structure of the albumin and the microenvironment around tyrosine and tryptophan residues. Competitive binding studies indicated Sudlow’s site I as the main protein pocket and molecular docking results suggested hydrogen bonding and hydrophobic interactions as the main binding forces.

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Design, Synthesis, in Vitro, and in Silico Evaluation of N‐Phenylacetamide‐Oxindole‐Thiosemicarbazide Hybrids as New Potential Tyrosinase Inhibitors

Boroujeni

Haghighijoo

Mohammadi‐Khanaposhtani

et al. 2022

Chemistry & Biodiversity

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A novel series of N‐phenylacetamide‐oxindole‐thiosemicarbazide hybrids were synthesized and evaluated for their tyrosinase inhibitory activity. According to tyrosinase inhibition results, all the synthesized compounds showed high tyrosinase inhibitory activity with IC50 values ranging from 0.8 to 3.88 μM in comparison to positive control kojic acid with IC50 value of 36.32 μM. Among tested compounds, analog 7o, containing the 2‐methyl‐4‐nitrophenyl on N‐phenylacetamide moiety displayed superior tyrosinase inhibition. This compound was around 45‐fold more potent than kojic acid. The kinetic analysis of compound 7o demonstrated that this compound is a competitive inhibitor against tyrosinase. Docking study of this compound demonstrated that compound 7o interacted with critical histidine residues within tyrosinase active site.

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Synthesis, tyrosinase inhibition and transportation behavior of novel β-enamino thiosemicarbazide derivatives by human serum albumin

Cited by 45 publications

References 55 publications

Synthetic (E)-3-Phenyl-5-(phenylamino)-2-styryl-1,3,4-thiadiazol-3-ium Chloride Derivatives as Promising Chemotherapy Agents on Cell Lines Infected with HTLV-1

Synthetic (E)-3-Phenyl-5-(phenylamino)-2-styryl-1,3,4-thiadiazol-3-ium Chloride Derivatives as Promising Chemotherapy Agents on Cell Lines Infected with HTLV-1

Multi-Spectroscopic and Theoretical Analysis on the Interaction between Human Serum Albumin and a Capsaicin Derivative—RPF101

Design, Synthesis, in Vitro, and in Silico Evaluation of N‐Phenylacetamide‐Oxindole‐Thiosemicarbazide Hybrids as New Potential Tyrosinase Inhibitors

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