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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

Stern-Volmer plots (a) and Double logarithm plots (b) for the interaction of RSBs with BSA ([RSBs] = 0.00, 0.50, 1.00, 1.50, 2.00, 2.50   10-5 mol/L, [BSA] = 1.00   10-5 mol/L, T = 290 K).
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Figure 3: Stern-Volmer plots (a) and Double logarithm plots (b) for the interaction of RSBs with BSA ([RSBs] = 0.00, 0.50, 1.00, 1.50, 2.00, 2.50   10-5 mol/L, [BSA] = 1.00   10-5 mol/L, T = 290 K).

Mentions: The Stern-Volmer plots for the interaction of the three RSBs with BSA were shown in Figure 3(a), based on the measured fluorescence data and the corresponding KSV, Kq values were calculated (Table 2). Obviously, the rate constants of BSA quenching procedure initiated by RSBs (RS, ROV, RMS) are much greater than the maximum scatter collision quenching constant of the biomolecule (Kq = 2.0 × 1010 L/mol·s). This means that the possible fluorescence quenching mechanism of BSA by RSBs is not initiated by dynamic collision but potentially from static quenching.


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)

Stern-Volmer plots (a) and Double logarithm plots (b) for the interaction of RSBs with BSA ([RSBs] = 0.00, 0.50, 1.00, 1.50, 2.00, 2.50   10-5 mol/L, [BSA] = 1.00   10-5 mol/L, T = 290 K).
© Copyright Policy
Related In: Results  -  Collection

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

Figure 3: Stern-Volmer plots (a) and Double logarithm plots (b) for the interaction of RSBs with BSA ([RSBs] = 0.00, 0.50, 1.00, 1.50, 2.00, 2.50   10-5 mol/L, [BSA] = 1.00   10-5 mol/L, T = 290 K).
Mentions: The Stern-Volmer plots for the interaction of the three RSBs with BSA were shown in Figure 3(a), based on the measured fluorescence data and the corresponding KSV, Kq values were calculated (Table 2). Obviously, the rate constants of BSA quenching procedure initiated by RSBs (RS, ROV, RMS) are much greater than the maximum scatter collision quenching constant of the biomolecule (Kq = 2.0 × 1010 L/mol·s). This means that the possible fluorescence quenching mechanism of BSA by RSBs is not initiated by dynamic collision but potentially from static quenching.

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