Interactions of isoorientin and its Semi-synthetic analogs with human serum albumin

Wang, Wenliang; Gao, Derong; Zheng, Qiancheng; Zhao, Xinbing; Na, Risong; Wan, Xin-Sheng; Li, Qing X.

doi:10.1016/j.bioorg.2021.105319

Cited by 13 publications

(7 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Herein, the MRE value at 208 nm was used for calculation, using the formula (Eq. ( 10)) as follows: [36] a À helix % ð Þ ¼ À MRE 208 À 4000 33000 À 4000 � 100 (10) As presented in Figure 5C, the negative peaks of HSA at 208 nm increased slightly with the increase of PA concentration, whereas their position and shape had no changes. The α-helix content in HSA was computed to increase from 50.52 % to 53.00 % in HSA-PA system, and reached 56.67 % when the PA concentration was 6×10 À 5 M. According to the thermodynamic calculations described earlier, the force for combination of PA with HSA was mainly hydrogen bonds or Van der Waals forces.…”

Section: Spectrum Analysismentioning

confidence: 95%

“…( 7), F(λ) is fluorescence value of HSA, and ɛ(λ) represents extinction coefficient of PA at the wavelength λ. [36] The spectral overlap of the fluorescence emission of HSA and the UV of PA were shown in Figure 3A visually. The values of J, R 0 and r (at the ratio of [HSA]: [Q] = 1 : 1) were obtained respectively according to Eq.…”

Section: Energy Transfer and Binding Distance For Hsa-pa Systemmentioning

confidence: 95%

See 1 more Smart Citation

Assessment of the Binding of Pseudallecin A to Human Serum Albumin with Multi‐Spectroscopic Analysis, Molecular Docking and Molecular Dynamic Simulation

Li,

Chen,

Qin

et al. 2023

Chemistry & Biodiversity

View full text Add to dashboard Cite

The binding of pseudallecin A (PA), a potential antibiotic with strong inhibitory activities against Gram‐positive Escherichia coli and Gram‐negative Staphylococcus aureus, to human serum albumin (HSA) was explored. The interaction between them was assessed by multi‐spectroscopic analysis, binding site competitive analysis, molecular docking and molecular dynamic simulation, showing the results as follows: PA effectively quenched the innate fluorescence of HSA by a static quenching process, formed a complex at a molar ratio of approximately 1:1 and performed an effective non‐radiative energy transfer; the binding of PA to HSA was a spontaneous exothermic reaction driven by enthalpy with strong affinity and had a slight effect on the conformation of HSA; PA bound at site Ⅲ of HSA and hydrogen bonds were the major binding forces to maintain the stability of the PA‐HSA complex. Molecular dynamic simulation was performed to calculate the root mean square deviation (RMSD), root mean square fluctuation (RMSF) and radius of gyration (Rg) for this complex and effectively supported the spectroscopic outcome. These results meant that the delivery and distribution of PA as a water‐insoluble molecule can be efficiently accomplished via HSA in human blood and, it has a good potential for future drug application and pharmacological development.

show abstract

Section: Spectrum Analysismentioning

confidence: 95%

Section: Energy Transfer and Binding Distance For Hsa-pa Systemmentioning

confidence: 95%

Assessment of the Binding of Pseudallecin A to Human Serum Albumin with Multi‐Spectroscopic Analysis, Molecular Docking and Molecular Dynamic Simulation

Li,

Chen,

Qin

et al. 2023

Chemistry & Biodiversity

View full text Add to dashboard Cite

show abstract

“…The thiazoles presented values that varied from 3.09x10 4 to 1.06 x10 5 L/mol. The higher the value of the constants, the stronger the binding of the compounds with theprotein (Wang et al 2021;Szymaszek et al 2022). Thus, the Ksv values suggest that the compounds that bound more strongly to the protein follow the following order of strength: 4 > 12 > 6 > 14 > 8 > 11 > 3 > 9 > 13 > 7 > 5 > 10.…”

Section: Interaction Assays Of Compounds With Human Albumin (Hsa)mentioning

confidence: 99%

“…The curves obtained in Figure 4 show that the fluorescence intensity of the protein (HSA) showed a gradual decrease in the intensity of maximum fluorescence emission of HSA at different concentrations of the compounds. The increase in the concentration of these compounds in solution causes the suppression of fluorescence emission (hypochromic effect) of the tryptophan amino acid residue of the protein, this is a clear indication of an interaction between HSA and the compounds (Alves et al 2021;Wang et al 2021). In addition, a slight shift in the albumin fluorescence emission band to the blue region (hypsochromic effect) was also observed, indicating the occurrence of interactions of the compound in the hydrophobic cavity of albumin, causing small structural changes in this region (Alves et al 2021;Wang et al 2021;Szymaszek et al 2022).The results presented in Table 2 show that the compounds were able to promote 100% fluorescence inhibition (hypochromism).…”

Section: Interaction Assays Of Compounds With Human Albumin (Hsa)mentioning

confidence: 99%

“…Thus, the Ksv values suggest that the compounds that bound more strongly to the protein follow the following order of strength: 4 > 12 > 6 > 14 > 8 > 11 > 3 > 9 > 13 > 7 > 5 > 10. In studies of interaction with human serum albumin (HSA), the Ksv values found were of the order of 10 4 and 10 5 , indicating that the interactions of the compounds with albumin are moderate to high (Alves et al 2021;Wang et al 2021;Szymaszek et al 2022).…”

Section: Interaction Assays Of Compounds With Human Albumin (Hsa)mentioning

confidence: 99%

See 1 more Smart Citation

Preliminary evaluation of the interaction with Albumin/DNA and in vitro evaluation of the antioxidant properties promoted by thiosemicarbazones and thiazole compounds

Nascimento,

Santos,

Pereira

et al. 2024

Sci. Electronic Arch

View full text Add to dashboard Cite

Thiosemicarbazones and thiazoles are known for their diverse biological activities. This study introduced two series of molecules, 4-(3-(4-nitrophenyl)-4-phenylthiazol-2(3H)-ylidene)-hydrazine)-methyl)-phenol and 4-(3-(4-chlorophenyl)-4-phenylthiazol-2(3H)-ylidene)-hydrazine)-methyl)-phenol, which exhibit biological potential as antioxidant agents. The study also assessed the interaction of these compounds with various HSA/DNA macromolecules. The results of the antioxidant activity showed that thiazoles in the DPPH assay exhibited IC50 values ranging from 439.4 to 691.67 µM. In the ABTS assay, thiosemicarbazones exhibited significant activity, ranging from 39.19 to 50.03 µM. Interaction assays were carried out with human serum albumin (HSA) and DNA. All compounds were able to interact with both DNA (low to moderate interaction) and HSA (moderate to high interaction).

show abstract

Novel Bis(2‐cyanoacrylamide) Linked to Sulphamethoxazole: Synthesis, DNA Interaction, Anticancer, ADMET, Molecular Docking, and DFT Studies

Ragheb,

Mohamed,

Diab

et al. 2024

Chemistry & Biodiversity

View full text Add to dashboard Cite

In the light of advancement and potential extensive use of medication design and therapy, new bis(cyanoacrylamides) incorporating sulphamethoxazole derivatives (7a‐7f) were synthesized and confirmed by different spectral tools. In vitro anticancer activity towards different human cancer cells (HCT116, MDA‐MB‐231 and A549) was assessed using MTT assay. Among all derivatives, 4C‐ and 6C‐spacer derivatives (7e and 7f) had the most potent growth inhibitory activities against HCT116 cells with IC50 values of 39.7 and 28.5 µM, respectively. 7e and 7f induced apoptosis and suppressed migration of HCT116 cells. These compounds also induced a significant increase in caspase‐3 activities, and downregulation of Bcl2 and CDH1 using ELISA. pBR322 DNA cleavage activities of cyanoacrylamides were determined using agarose gel electrophoresis. Furthermore, 7e and 7f showed good DNA and BSA binding affinities using different spectroscopic techniques. Furthermore, molecular docking for 7e and 7f was performed to anticipate their binding capabilities toward various proteins (Bcl2, CDH1 and BSA). The docking results were well correlated with those of experimental results. Additionally, density functional theory and ADMET study were performed to evaluate the molecular and pharmacokinetic features of 7e and 7f, respectively. Thus, this work reveals promising antitumor lead compounds that merit future research and activity enhancement.

show abstract

Interactions of isoorientin and its Semi-synthetic analogs with human serum albumin

Cited by 13 publications

References 44 publications

Assessment of the Binding of Pseudallecin A to Human Serum Albumin with Multi‐Spectroscopic Analysis, Molecular Docking and Molecular Dynamic Simulation

Assessment of the Binding of Pseudallecin A to Human Serum Albumin with Multi‐Spectroscopic Analysis, Molecular Docking and Molecular Dynamic Simulation

Preliminary evaluation of the interaction with Albumin/DNA and in vitro evaluation of the antioxidant properties promoted by thiosemicarbazones and thiazole compounds

Novel Bis(2‐cyanoacrylamide) Linked to Sulphamethoxazole: Synthesis, DNA Interaction, Anticancer, ADMET, Molecular Docking, and DFT Studies

Contact Info

Product

Resources

About