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Synthesis of three rimantadine schiff bases and their biological effects on serum albumin.

Liu BM, Ma P, Wang X, Kong YM, Zhang LP, Liu B - Iran J Pharm Res (2014)

Bottom Line: The results showed that the three RSBs effectively quenched the intrinsic fluorescence of BSA via static quenching.According to the results of displacement experiments of site probes, it was considered that the binding sites were located in hydrophobic cavities in sub-domains IIA of BSA.What is more, synchronous fluorescence studies indicated that the hydrophobicity around tryptophan residues was increased with the addition of rimantadine-o-vanillin (ROV) and rimantadine-4-methoxy-salicylaldehyde (RMS), while there was no apparent change with the addition of rimantadine-salicylaldehyde (RS).

View Article: PubMed Central - PubMed

Affiliation: College of Pharmacy , Liaoning University, Shenyang 110036, P . R . China .

ABSTRACT
Three new rimantadine Schiff bases (RSBs) were prepared, and then the interaction of RSBs with bovine serum albumin (BSA) was investigated using fluorescence, synchronous fluorescence, UV-vis absorption spectroscopy under physiological conditions. The results showed that the three RSBs effectively quenched the intrinsic fluorescence of BSA via static quenching. Binding constant (K a), number of binding sites (n), and the binding distance (r) between three RSBs and BSA were calculated by Stern-Volmer equation and Förster's theory in this study. According to the results of displacement experiments of site probes, it was considered that the binding sites were located in hydrophobic cavities in sub-domains IIA of BSA. What is more, synchronous fluorescence studies indicated that the hydrophobicity around tryptophan residues was increased with the addition of rimantadine-o-vanillin (ROV) and rimantadine-4-methoxy-salicylaldehyde (RMS), while there was no apparent change with the addition of rimantadine-salicylaldehyde (RS).

No MeSH data available.


Related in: MedlinePlus

Synchronous fluorescence quenching spectra of BSA in the presence of RSBs (RS, ROV, RMS). ([RSBs] (a→f) = 0.00, 0.50, 1.00, 1.50, 2.00, 2.50   10-5 mol/L; [BSA] = 1.00   10-5 mol/L).
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Figure 6: Synchronous fluorescence quenching spectra of BSA in the presence of RSBs (RS, ROV, RMS). ([RSBs] (a→f) = 0.00, 0.50, 1.00, 1.50, 2.00, 2.50   10-5 mol/L; [BSA] = 1.00   10-5 mol/L).

Mentions: Synchronous fluorescence measurements provide information about the molecular microenvironment in the vicinity of the fluorophore functional groups. The maximum emission wavelengths of the residues are related to the polarity of the surrounding environment. Synchronous fluorescence spectra were obtained by simultaneously scanning excitation and emission monochromators. If Δλ = 15 nm, the synchronous fluorescence spectrum exhibits the spectral character only of tyrosine residues, and if Δλ = 60 nm, it exhibits that only of tryptophan residues. Synchronous fluorescence spectra of BSA upon addition of RSBs (RS, ROV, RMS) gained at Δλ = 15 and 60 nm were shown in Figure 6.


Synthesis of three rimantadine schiff bases and their biological effects on serum albumin.

Liu BM, Ma P, Wang X, Kong YM, Zhang LP, Liu B - Iran J Pharm Res (2014)

Synchronous fluorescence quenching spectra of BSA in the presence of RSBs (RS, ROV, RMS). ([RSBs] (a→f) = 0.00, 0.50, 1.00, 1.50, 2.00, 2.50   10-5 mol/L; [BSA] = 1.00   10-5 mol/L).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4232783&req=5

Figure 6: Synchronous fluorescence quenching spectra of BSA in the presence of RSBs (RS, ROV, RMS). ([RSBs] (a→f) = 0.00, 0.50, 1.00, 1.50, 2.00, 2.50   10-5 mol/L; [BSA] = 1.00   10-5 mol/L).
Mentions: Synchronous fluorescence measurements provide information about the molecular microenvironment in the vicinity of the fluorophore functional groups. The maximum emission wavelengths of the residues are related to the polarity of the surrounding environment. Synchronous fluorescence spectra were obtained by simultaneously scanning excitation and emission monochromators. If Δλ = 15 nm, the synchronous fluorescence spectrum exhibits the spectral character only of tyrosine residues, and if Δλ = 60 nm, it exhibits that only of tryptophan residues. Synchronous fluorescence spectra of BSA upon addition of RSBs (RS, ROV, RMS) gained at Δλ = 15 and 60 nm were shown in Figure 6.

Bottom Line: The results showed that the three RSBs effectively quenched the intrinsic fluorescence of BSA via static quenching.According to the results of displacement experiments of site probes, it was considered that the binding sites were located in hydrophobic cavities in sub-domains IIA of BSA.What is more, synchronous fluorescence studies indicated that the hydrophobicity around tryptophan residues was increased with the addition of rimantadine-o-vanillin (ROV) and rimantadine-4-methoxy-salicylaldehyde (RMS), while there was no apparent change with the addition of rimantadine-salicylaldehyde (RS).

View Article: PubMed Central - PubMed

Affiliation: College of Pharmacy , Liaoning University, Shenyang 110036, P . R . China .

ABSTRACT
Three new rimantadine Schiff bases (RSBs) were prepared, and then the interaction of RSBs with bovine serum albumin (BSA) was investigated using fluorescence, synchronous fluorescence, UV-vis absorption spectroscopy under physiological conditions. The results showed that the three RSBs effectively quenched the intrinsic fluorescence of BSA via static quenching. Binding constant (K a), number of binding sites (n), and the binding distance (r) between three RSBs and BSA were calculated by Stern-Volmer equation and Förster's theory in this study. According to the results of displacement experiments of site probes, it was considered that the binding sites were located in hydrophobic cavities in sub-domains IIA of BSA. What is more, synchronous fluorescence studies indicated that the hydrophobicity around tryptophan residues was increased with the addition of rimantadine-o-vanillin (ROV) and rimantadine-4-methoxy-salicylaldehyde (RMS), while there was no apparent change with the addition of rimantadine-salicylaldehyde (RS).

No MeSH data available.


Related in: MedlinePlus