Iron ligand recognition by monomeric hemoglobins

Stephanos, Joseph J.; Farina, Scott A.; Addison, Anthony W.

doi:10.1016/0167-4838(96)00041-6

Cited by 37 publications

(31 citation statements)

References 58 publications

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“…From the Fig. 5b, the plot between 1/ (A obs -A 0 ) versus 1/[5FU-NPs] was found to be linear with binding constant as (9.37 ± 0.67) 9 10 2 M -1 (Stephanos et al 1996;Chinnathambi et al 2014).…”

Section: Uv-visible Absorption Studiesmentioning

confidence: 95%

Synthesis of 5-Fluorouracil conjugated LaF3:Tb3+/PEG-COOH nanoparticles and its studies on the interaction with bovine serum albumin: spectroscopic approach

et al. 2015

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The luminescent lanthanide-doped nanoparticles have gathered considerable attention in many fields especially in biomedicine. In this work, the lanthanum fluoride-doped terbium nanoparticles (LaF 3 :Tb 3? NPs) via simple chemical precipitation method has been synthesized and functionalized with polyethylene glycol. The size and the shape of the nanoparticles are confirmed using X-ray diffraction and transmission electron microscopy. The conjugation of 5-Fluorouracil (5-FU) and thus synthesized nanoparticles (NPs) were confirmed using various spectroscopic methods such as UVVisible spectroscopy, fluorescence steady state, and excited state spectroscopy studies. The enhancement in fluorescence emission (k = 543 nm) of drug-conjugated nanoparticles confirms the Vander Waals force of attraction due to F-F bonding between the drug and the nanoparticles. Further, the effects of 5FU-NPs in carrier protein were investigated using bovine serum albumin as a protein model. The 5FU-LaF 3 :Tb 3? nanoparticles binding is illustrated with binding constant and number of binding sites. The structural change of bovine serum albumin has been studied using circular dichroism and Fourier transform infrared spectroscopy analysis. Graphical AbstractKeywords Lanthanum fluoride Á 5-Fluorouracil Á Serum albumin Á Fluorescence quenching Á Vander Waal force of attraction

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Section: Uv-visible Absorption Studiesmentioning

confidence: 95%

Synthesis of 5-Fluorouracil conjugated LaF3:Tb3+/PEG-COOH nanoparticles and its studies on the interaction with bovine serum albumin: spectroscopic approach

et al. 2015

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“…The intrinsic constant for the binding of insulin with IBA was calculated according to the methods described by Benesi-Hildebrand, based on the equation (1) [10,11]. (Fig.…”

Section: Uv-vis Measurementsmentioning

confidence: 99%

Spectroscopic study of the interaction of insulin and its aptamer – sensitive optical detection of insulin

Verdian

Housaindokht

2015

Journal of Luminescence

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“…drug = AZT, cis-Pt, aspirin and ascorbate anion The values of the binding constants K were obtained from the protein absorption at 270 nm according to the method described by published methods [23,24] where the bindings of various ligands to hemoglobin were described. For weak binding affinities the data were treated using linear reciprocal plots based on 0 0 0…”

Section: Uv-vis Absorption Spectramentioning

confidence: 99%

“…Thus, the double reciprocal plot of 1/(A -A 0 ) vs. 1/C ligand is linear and the binding constant (K) can be estimated from the ratio of the intercept to the slope [23,24].…”

Section: Uv-vis Absorption Spectramentioning

confidence: 99%

Flexibility of Na,K-ATPase secondary structure upon drug-protein interaction

Tajmir-Riahi

2007

JICS

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The enzyme Na + , K + -ATPase is an integral membrane protein which transports sodium and potassium cations against an electrochemical gradient. The transport of Na + and K + ions is connected to an oscillation of the enzyme between the two conformational states, the E 1 (Na + ) and the E 2 (K + ) conformations. The enzymatic activity of ATPase is largley affected by different ligands complexation. This review reports the effects of several drugs such as AZT (anti-AIDS), cis-Pt (antitumor), aspirin (anti-inflammatory) and vitamin C (antioxidant) on the stability and secondary structure of Na,K-ATPase in vitro. Drugenzyme binding is mainly through H-bonding to the polypeptide C=O and C-N groups with two binding constants K 1(AZT) = 5.30 × 10 5 M -1 and K 2(AZT) = 9.80 × 10 3 M -1 for AZT and one binding constant for K cis-Pt = 1.93 × 10 4 M -1 , K aspirin = 6.45 × 10 3 M -1 and K ascorbate = 1.04 × 10 4 M -1 for cis-Pt, aspirin and ascorbic acid. The enzyme secondary structure was altered from that of α-helix 19.8% (free protein) to almost 22-26% and the β-sheet from 25.6% to 18-22%, upon drug complexation with the order of induced stability AZT > cis-Pt > ascorbate > aspirin.

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Iron ligand recognition by monomeric hemoglobins

Cited by 37 publications

References 58 publications

Synthesis of 5-Fluorouracil conjugated LaF3:Tb3+/PEG-COOH nanoparticles and its studies on the interaction with bovine serum albumin: spectroscopic approach

Synthesis of 5-Fluorouracil conjugated LaF3:Tb3+/PEG-COOH nanoparticles and its studies on the interaction with bovine serum albumin: spectroscopic approach

Spectroscopic study of the interaction of insulin and its aptamer – sensitive optical detection of insulin

Flexibility of Na,K-ATPase secondary structure upon drug-protein interaction

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