Metal Ions Enhance the Affinities of Flavonoids for Human Serum Albumin in Vitro

Yang, Fan; Wang, Jie; Liu, Chunxi; Xü, Xinsheng; Shan, Shunan; Zhi-hua, Xia; Sun, Xiaowei

doi:10.1007/s10953-012-9846-z

Cited by 6 publications

(3 citation statements)

References 26 publications

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“…[305][306][307][308] While several studies have investigated the structure-activity relationships for avonoid-SA binding, [309][310][311][312][313][314] interactions between SA and avonoid metal complexes are much less well explored. An increase 315 as well as a decrease 161,316,317 in affinity upon complexation was observed. This may be dependent on whether all the coordination sites are saturated.…”

Section: Interaction With Serum Albuminmentioning

confidence: 89%

Properties and applications of flavonoid metal complexes

2015

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Section: Interaction With Serum Albuminmentioning

confidence: 89%

Properties and applications of flavonoid metal complexes

2015

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“…The association constants and the number of the binding sites of MB binding to HSA in the presence of Cu 2+ and Fe 3+ are calculated by eqn 2, which are shown in Fig. 9 and listed in number of sites leads to an increase of the amount of ligand bound to HSA (57). Thus the presence of Cu 2+ and Fe 3+ may result in a decrease in the free, biologically active fraction of MB in plasma and thus decrease its maximum effects and prolong the storage period of MB in plasma.…”

Section: Influences Of Cu 2+ and Fe 3+ On The Association Constants Amentioning

confidence: 99%

Enhancement of the binding affinity of methylene blue to site I in human serum albumin by cupric and ferric ions

Wang

et al. 2015

Luminescence

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In this work, the binding characteristics of methylene blue (MB) to human serum albumin (HSA) and the influence of Cu(2+) and Fe(3+) on the binding affinity of MB to HSA were investigated using fluorescence, absorption, circular dichroism (CD) spectroscopy and molecular modelling. The results of competitive binding experiments using the site probes ketoprofen and ibuprofen as specific markers suggested that MB was located in site I within sub-domain IIA of HSA. The molecular modelling results agreed with the results of competitive site marker experiments and the results of CD spectra indicated that the interaction between MB and HSA caused the conformational changes in HSA. The binding affinity of MB to HSA was enhanced but to a different extent in the presence of Cu(2+) and Fe(3+), respectively, which indicated that the influence of different metal ions varied. Enhancement of the binding affinity of MB to HSA in the presence of Cu(2+) is due to the formation of Cu(2+)-HSA complex leading to the conformational changes in HSA, whereas in the presence of Fe(3+), enhancement of the binding affinity is due to the greater stability of the Fe(3+)-HSA-MB complex compared with the MB-HSA complex.

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“…The results suggest that weakly cationic peptides benefit most from PP1 conjugation. It has been reported that there is a cooperative effect of metal ions on the binding of hydrophobic compounds to HSA, and the structural influence of Zn 2+ ions could in principle also play a role in the binding of hydrophobic peptides . This is unlikely to play a significant role in our case, as 4‐C15L8‐Ac did not bind HSA in the presence of ZnCl 2 (Figure S2).…”

Section: Resultsmentioning

confidence: 67%

Conjugation of a Dipicolyl Chelate to Polypeptide Conjugates Increases Binding Affinities for Human Serum Albumin and Survival Times in Human Serum

Balliu

Baltzer

2017

ChemBioChem

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The affinity for human serum albumin (HSA) of a series of 2-5 kDa peptides covalently linked to 3,5-bis[[bis(2-pyridylmethyl)amino]methyl]benzoic acid, a dipicolyl chelator with micromolar affinity for Zn , was found by surface plasmon resonance to increase in the presence of 1 μm ZnCl at physiological pH. The dependence on polypeptide hydrophobicity was found to be minor, thus suggesting that the conjugates bound to the metal-binding site and not to the fatty-acid-binding site. The affinity of the conjugates increased strongly with the positive charge of the polypeptides, thus implicating the negatively charged protein surface surrounding the metal-binding site. The survival times of the peptides in human serum were extended as a consequence of stronger binding to HSA, thus suggesting that Zn -chelating agents might provide a general route to increased survival time of peptides in serum in therapeutic and diagnostic applications without significantly increasing their molecular weights.

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Metal Ions Enhance the Affinities of Flavonoids for Human Serum Albumin in Vitro

Cited by 6 publications

References 26 publications

Properties and applications of flavonoid metal complexes

Properties and applications of flavonoid metal complexes

Enhancement of the binding affinity of methylene blue to site I in human serum albumin by cupric and ferric ions

Conjugation of a Dipicolyl Chelate to Polypeptide Conjugates Increases Binding Affinities for Human Serum Albumin and Survival Times in Human Serum

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