16 research outputs found
Steady State and Time Resolved Emission of TC in Various Solvents.
<p>(<b>A</b>) Fluorescence spectra of TC (25 µM) at 298 K in (1) water, (2) ethanol (EtOH), (3) isopropanol (iPrOH), (4) ethylene glycol (EG), (5) dimethylformamide (DMF), (6) dimethyl sulphoxide (DMSO); λ<sub>exc</sub> = 370 nm; excitation and emission band pass = 10 nm and 5 nm respectively. (<b>B</b>) Fluorescence decay of TC (25 µM) at 298 K in (B) EtOH, iPr-OH, EG, DMF, DMSO; λexc = 370 nm; excitation and emission bandpass = 10 nm each.</p
Plot of φ (A) and <τ> (B) against (I) dielectric constant (ε), (II) solvent polarizability parameter (π*), (III) Hydrogen bond donating ability (α) of different solvents, (1) DMSO, (2) DMF, (3) EG, (4) EtOH, (5) i-PrOH.
<p>Plot of φ (A) and <τ> (B) against (I) dielectric constant (ε), (II) solvent polarizability parameter (π*), (III) Hydrogen bond donating ability (α) of different solvents, (1) DMSO, (2) DMF, (3) EG, (4) EtOH, (5) i-PrOH.</p
The Changes in Accessible Surface Area (ΔASA)<sup>a</sup> of the Residues of Serum Albumins after Complexed with Tetracycline.
a<p>ΔASA<sub>i</sub> = ASA<sup>i</sup><sub>HSA/BSA</sub> – ASA<sup>i</sup><sub>HSA/BSA – TC complex.</sub></p
Fluorescence anisotropy decays of TC (25 µM) at 298 K in pure EG.
<p>I<sub>VV</sub> and I<sub>VH</sub> represent decays of emission of TC with excitation polarizer at vertical position and emission polarizer at vertical and horizontal position, respectively. λ<sub>exc</sub> = 370 nm; excitation and emission band pass = 10 nm each.</p
Variation of (I) fluorescence quantum yield (φ).
<p>(II) fluorescence anisotropy (r); (III) singlet state average lifetime (τ) of TC (25 µM) in aqueous buffer with increasing concentration of serum albumins. (A) for BSA, (B) for HSA.</p
Docked poses of serum albumin-TC complexes.
<p>(A) The surrounding amino acid residues of (I) BSA (II) HSA within 5 Ã… from TC. (B) Distances (in Ã…) obtained from docked poses of different Trp residue/s of (I) BSA (II) HSA from TC.</p
Phosphorescence Data for Wild-Type Serum Albumins and its Complex with TC in a 40% Ethylene Glycol Matrix at 77 K (λ<sub>exc</sub> = 280 nm).
<p>Phosphorescence Data for Wild-Type Serum Albumins and its Complex with TC in a 40% Ethylene Glycol Matrix at 77 K (λ<sub>exc</sub> = 280 nm).</p
Singlet State Lifetime and Quantum Yield of TC (25 µM) as a Function of Added Concentration of Serum Albumins with λ<sub>ex</sub> = 370 nm at 298 K.
<p>Singlet State Lifetime and Quantum Yield of TC (25 µM) as a Function of Added Concentration of Serum Albumins with λ<sub>ex</sub> = 370 nm at 298 K.</p
Binding Constant (K<sub>b</sub>) and Free Energy Change (ΔG) Associated with Binding Following Different Methods at 298 K.
a<p>Ref <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0060940#pone.0060940-Anand1" target="_blank">[66]</a>.</p>b<p>Ref <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0060940#pone.0060940-Mukherjee1" target="_blank">[20]</a>.</p
The plot of (A) (I) [F<sub>∞</sub> − F<sub>0</sub>]/[F<sub>x</sub> − F<sub>0</sub>] against [BSA]<sup>−1</sup>(II) (r−r<sub>f</sub>)/R(r<sub>b</sub>−r) against [BSA]; (B) (I) and (II) similar plot for HSA.
<p>The plot of (A) (I) [F<sub>∞</sub> − F<sub>0</sub>]/[F<sub>x</sub> − F<sub>0</sub>] against [BSA]<sup>−1</sup>(II) (r−r<sub>f</sub>)/R(r<sub>b</sub>−r) against [BSA]; (B) (I) and (II) similar plot for HSA.</p