Interaction of some water-soluble metalloporphyrazines with human serum albumin

Asadi, Mozaffar; Bordbar, Abdol‐Khalegh; Safaei, Elham; Ghasemi, Jahan B.

doi:10.1016/j.molstruc.2004.03.052

Cited by 28 publications

(5 citation statements)

References 30 publications

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“…The choice was based on the observation that 4.8 ns is the longest lifetime component previously detected in horse heart myoglobin and now present in hemoglobin [25]. It is also consistent with the dominant lifetime component exhibited by tryptophan in a water environment and embedded in other proteins, such as human albumin serum [26] and bovine albumin serum [27]. Fig.…”

Section: Fluorescence Quenching Mechanismmentioning

confidence: 82%

Investigation of the interaction between colloidal TiO2 and bovine hemoglobin using spectral methods

Wang

Zhang

Wang

2008

Colloids and Surfaces B: Biointerfaces

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Section: Fluorescence Quenching Mechanismmentioning

confidence: 82%

Investigation of the interaction between colloidal TiO2 and bovine hemoglobin using spectral methods

Wang

Zhang

Wang

2008

Colloids and Surfaces B: Biointerfaces

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“…cooperative, competitive, non‐competitive) . Serum albumin binds drugs via one of two possible binding sites: Site 1 utilizes hydrophobic interactions to affiliate bulky, heterocyclic molecules of negative charge, and Site 2 requires the presence of aromatic carboxyl groups bearing strong negative charge and situated far from any non‐polar regions of the drug . As such, a number of studies have highlighted human and bovine serum albumin as solubilization and drug carriers for various Ps .…”

Section: Shortcomings Of Current Photosensitizers For Phototherapymentioning

confidence: 99%

“…Serum albumin binds drugs via one of two possible binding sites: Site 1 utilizes hydrophobic interactions to affiliate bulky, heterocyclic molecules of negative charge, and Site 2 requires the presence of aromatic carboxyl groups bearing strong negative charge and situated far from any non‐polar regions of the drug . As such, a number of studies have highlighted human and bovine serum albumin as solubilization and drug carriers for various Ps . Studies have distinguished entropy driven associations behind the albumin binding affinity for Ps that creates a “goldilocks” scenario, sufficient binding strength for stable complex formation which also allows release thereof at the drug target site. Ps binding to lipoproteins, particularly low‐density Lipoproteins (LDL), has attracted attention not only for enhanced solubility but also for its targeted intracellular localization capabilities.…”

Section: Shortcomings Of Current Photosensitizers For Phototherapymentioning

confidence: 99%

Mechanistics and photo‐energetics of macrocycles and photodynamic therapy: An overview of aspects to consider for research

Horne

Cronjé

2017

Chem Biol Drug Des

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Research within the field of photodynamic therapy has escalated over the past 20 years. The required conjunctional use of photosensitizers, particularly of the macrocycle structure, has lead to a vast repertoire of derivatives that branch classes and subclasses thereof. Each exhibits a differential range of physiochemical properties that influence their potential applications within the larger phototherapy field for use in either diagnostics, photodynamic therapy, both or none. Herein, we provide an overview of these properties as they relate to photodynamic therapy and to a lesser extent diagnostics. By summarizing the mechanistics of photodynamic therapy coupled to the photo-energetics displayed by macrocycle photosensitizers, we aimed to highlight the critical aspects any researcher should be aware of and consider when selecting and performing research for therapeutic application purposes. These include photosensitizer, photophysical and structural properties, synthesis design and subsequent attributes, main applications within research, common shortcomings exhibited and the current methods practiced to overcome them. K E Y W O R D Sco

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“…We have previously reported the spectroscopic studies to characterize the interactions of some drugs with serum albumin [1,3]. In this study to elucidate the binding behavior of nickel (II) tetrasulfonated phthalocyanine anion Ni(tspc) 4− ( Fig.…”

Section: Introductionmentioning

confidence: 99%

Thermodynamic characterization of phthalocyanine–human serum albumin interaction

2011

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The thermodynamic of the binding of nickel (II) tetrasulfonated phthalocyanine anion [Ni(tspc)4–], to human serum albumin (HSA) was investigated in 5 mM aqueous phosphate buffer of pH 7.40 at 25°C using optical absorption spectroscopy. The results show that [Ni(tspc)4–] does not have any affinity for aggregation due to increasing of salt concentration and exists as monomers even in homogeneous aqueous solutions of high ionic strengths (more than 2 M NaCl). The binding constant (K) was obtained by analysis of optical absorption spectra of mentioned complex at various HSA concentrations using SQUAD software. The value ofKwas estimated to be 4.89×105±0.03 (M–1) at 25°C. The thermodynamic parameters were calculated by van’t Hoff equation. The enthalpy and entropy changes were 28.08 kJ/mol and 203.09 J/(mol?·?K) at 25°C, respectively. The results indicate that the binding is mainly entropy driven and the enthalpy is unfavorable for it, the hydrophobic forces thus playing a major role in the binding process.

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Interaction of some water-soluble metalloporphyrazines with human serum albumin

Cited by 28 publications

References 30 publications

Investigation of the interaction between colloidal TiO2 and bovine hemoglobin using spectral methods

Investigation of the interaction between colloidal TiO2 and bovine hemoglobin using spectral methods

Mechanistics and photo‐energetics of macrocycles and photodynamic therapy: An overview of aspects to consider for research

Thermodynamic characterization of phthalocyanine–human serum albumin interaction

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