Limits...
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

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
getmorefigures.php?uid=PMC4232783&req=5

Figure 2: 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: Figure 2 shows the emission spectra of BSA in the absence and presence of RSBs (RS, ROV, RMS). As can be seen from Figure 2, BSA had strong fluorescence emission with a peak at 340 nm on excitation at 280 nm. Furthermore, the addition of RSBs led to a concentration-dependent quenching of BSA intrinsic fluorescence intensity and the maximum emission wavelengths were slightly shifted from 340 nm to 337 nm for RS and ROV, 340 nm to 336 nm for RMS. These results indicate that the binding of RSBs to BSA occurs and the microenvironment around chromophore of BSA is changed upon addition of RSBs (RS, ROV, RMS).


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)

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 2: 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: Figure 2 shows the emission spectra of BSA in the absence and presence of RSBs (RS, ROV, RMS). As can be seen from Figure 2, BSA had strong fluorescence emission with a peak at 340 nm on excitation at 280 nm. Furthermore, the addition of RSBs led to a concentration-dependent quenching of BSA intrinsic fluorescence intensity and the maximum emission wavelengths were slightly shifted from 340 nm to 337 nm for RS and ROV, 340 nm to 336 nm for RMS. These results indicate that the binding of RSBs to BSA occurs and the microenvironment around chromophore of BSA is changed upon addition of RSBs (RS, ROV, RMS).

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