2010
DOI: 10.1016/j.jlumin.2010.02.014
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Characterization of the interaction between human lactoferrin and lomefloxacin at physiological condition: Multi-spectroscopic and modeling description

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Cited by 74 publications
(29 citation statements)
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“…The observed fluorescence quenching of Trp and Try residues suggested that the HSA-ligand interaction changed the micro-environment of these residues. Moreover, the blue shift in the fluorescence spectra corresponded to a decreased polarity of the micro-environment after binding, which indicated that the chromophore of the protein was brought to more hydrophobic surroundings [24]. The quenching of HSA fluorescence by any ligand leads to the conclusion that this ligand can bind in the IIA sub-domain since in this albumin there is only one Trp, located in the IIA sub-domain.…”
Section: Fluorescence Quenching Of Hsa By Asa and Aml In Binary And Tmentioning
confidence: 99%
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“…The observed fluorescence quenching of Trp and Try residues suggested that the HSA-ligand interaction changed the micro-environment of these residues. Moreover, the blue shift in the fluorescence spectra corresponded to a decreased polarity of the micro-environment after binding, which indicated that the chromophore of the protein was brought to more hydrophobic surroundings [24]. The quenching of HSA fluorescence by any ligand leads to the conclusion that this ligand can bind in the IIA sub-domain since in this albumin there is only one Trp, located in the IIA sub-domain.…”
Section: Fluorescence Quenching Of Hsa By Asa and Aml In Binary And Tmentioning
confidence: 99%
“…This means that only the Trp residue participated in both the HSA-ASA and (HSA-AML)ASA interactions, which may suggest that in the presence of another ligand, the structure of HSA changed, rendering the quantitative analysis impossible. The fluorescence quenching behavior could be analyzed using the Stern-Volmer equation of linear fittings [24]. allowed us to determine the quenching constants K Q and f a for HSA-drug complexes [25].…”
Section: Fluorescence Quenching Of Hsa By Asa and Aml In Binary And Tmentioning
confidence: 99%
“…They are derived from the basic structure of nalidixic acid and have substituents at N‐1, C‐5, C‐7 at position 8 and a fluorine atom at position 6. Fluoroquinolones inhibit bacterial DNA gyrase and topoisomerase IV enzymes, resulting \in inhibition of DNA replication and transcription . The fluorine atom at position 6 enhances gyrase inhibition and cell penetration.…”
Section: Introductionmentioning
confidence: 99%
“…Fluoroquinolones inhibit the bacterial DNA gyrase or the topoisomerase IV enzyme, resulting the inhibition of DNA replication and transcription [4][5][6][7]. Fluorine atom at position 6 enhances gyrase inhibition and cell penetration.…”
Section: Introductionmentioning
confidence: 99%
“…Piperazinyl substituents provide activity against Gram-negative bacteria and pyrrolidinyl moity is active against Gram-positive cocci. The function substituted at position 8 is to control anaerobe activity [7].…”
Section: Introductionmentioning
confidence: 99%