2015
DOI: 10.1016/j.jlumin.2014.12.002
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Comparison of 9-hydroxy-artemisinin with artemisinin: interaction with bovine hemoglobin

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Cited by 9 publications
(6 citation statements)
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“…Suppressors are mostly polymers such as polyethylene glycol (PEG), [16][17][18] triblock copolymers, 19 polypropylene glycol (PPG) [20][21][22] or diallylamine-type copolymers. 23 These polymers interact with chloride ions to inhibit copper deposition.…”
mentioning
confidence: 99%
“…Suppressors are mostly polymers such as polyethylene glycol (PEG), [16][17][18] triblock copolymers, 19 polypropylene glycol (PPG) [20][21][22] or diallylamine-type copolymers. 23 These polymers interact with chloride ions to inhibit copper deposition.…”
mentioning
confidence: 99%
“…As explained previously, the interaction between formetanate hydrochloride and Hb exposes hydrophobic patches on protein surfaces to the solvent (20). Reduction of the CD intensity in the presence of formetanate hydrochloride elucidated that the insecticide may be able to induce conformational changes in the secondary structure of Hb (21,22) Based on the results of thermodynamic parameters and the negative values of both ∆H° and ∆S°, it can be concluded that the binding process is enthalpy driven and the hydrogen bonds and van der Waals forces are involved in the binding reaction and complex stability. In addition, the negative amount of ∆G° confirms that the binding process is spontaneous (23).…”
Section: / Khatibi Sharifiyeh and Colleaguesmentioning
confidence: 77%
“…The far-UV CD curve of hemoglobin exhibited two negative peaks in the far-UVCD region at 208 nm and 222 nm, which refer to ᴨ→ᴨ* transition of the α-helix and n→ᴨ* transition for both the α-helix and random coil, respectively (31). Upon binding to each seven dyes, the CD spectrum of Hb diminished in magnitude, suggesting the decrease in the helical content of Hb.…”
Section: CDmentioning
confidence: 99%
“…Decreasing the fluorescence intensity indicates the increase of polarity around aromatic residues such as Trp and Tyr, meaning that this interaction led protein to unfolding states. Due to the decrease in values of the K sv and K q along with raising temperature, the nature of Hb fluorescence quenching found to be static because increasing the temperature resulted in increment of the molecular collisions in dynamic quenching; accordingly, the values of K sv and K q raised with temperature (6,31). Unfolding of Hb as a result of interaction with La and Acs was more displayed by the far-UV CD results, which demonstrated that all these ionic metals caused loss of helicity in the protein and led that into structural instability.…”
Section: CDmentioning
confidence: 99%