The effect of porphyrin structure on binding to human serum albumin by fluorescence spectroscopy

Rinco, Olga; Brenton, Janet; Douglas, Alison J.; Maxwell, Amanda; Henderson, Michelle J.; Indrelie, Kirsten; Wessels, Jacob; Widin, Joan

doi:10.1016/j.jphotochem.2009.08.009

Cited by 44 publications

(26 citation statements)

References 18 publications

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“…Thus, the successive binding of Timolol should occur close to the Trp residue. A remarkable blue shift at the maximum wavelength (356‐346 nm) was also observed, which indicated the fall of polarity and the increase of hydrophobicity around Trp residues . The clear existence of an isobestic point at 346 nm suggested that there is an equilibrium between the free species and the HSA‐bound Timolol …”

Section: Resultsmentioning

confidence: 99%

“…Human serum albumin intramolecular forces and conformation can be affected and changed by small molecule binding . Most of the intrinsic fluorescence of HSA is attributed to Trp 214 . According to Figure 8, the fluorescence intensity of HSA decreased, and a very slight red shift (about 4) nm was observed for the emission wavelength with increasing propranolol concentration.…”

Section: Resultsmentioning

confidence: 99%

“…As seen, HSA has a was also observed, which indicated the fall of polarity and the increase of hydrophobicity around Trp residues. 19,20 The clear existence of an isobestic point at 346 nm suggested that there is an equilibrium between the free species and the HSA-bound Timolol. 21 Figure 6 illustrates the concentration profile of Timolol in connection with different incubation times.…”

Section: Timololmentioning

confidence: 99%

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Molecular interaction of some cardiovascular drugs with human serum albumin at physiological‐like conditions: A new approach

Niaei

Hasanzadeh

Shadjou

2018

J of Molecular Recognition

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In the present study, the interaction of human serum albumin (HSA) with some cardiovascular drugs (CARs) under physiological conditions was investigated via the fluorescence spectroscopic and Fourier transform infrared spectroscopy. The CAR included Captopril, Timolol, Propranolol, Atenolol, and Amiodarone. Cardiovascular drugs can effectively quench the endogenous fluorescence of HSA by static quenching mechanism. The fluorescence quenching of HSA is mainly caused by complex formation of HSA with CAR. The binding reaction of CAR with HSA can be concluded that hydrophobic and electrostatic interactions are the main binding forces in the CAR‐HSA system. The results showed that CAR strongly quenched the intrinsic fluorescence of HSA through a static quenching procedure, and nonradiation energy transfer happened within molecules. Fourier transform infrared spectroscopy absorption studies showed that the secondary structure was changed according to the interaction of HSA and CAR. The binding reaction of CAR with HSA can be concluded that hydrophobic and electrostatic interactions are the main binding forces in the CAR‐HSA system. The results obtained herein will be of biological significance in pharmacology and clinical medicines.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Timololmentioning

confidence: 99%

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Molecular interaction of some cardiovascular drugs with human serum albumin at physiological‐like conditions: A new approach

Niaei

Hasanzadeh

Shadjou

2018

J of Molecular Recognition

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“…When a porphyrin enters a living organism, it may combine with a protein such as HSA, and this will control its accumulation, distribution, and metabolism in the body. Therefore, there have been numerous studies on the interaction of porphyrins with HSA …”

Section: Introductionmentioning

confidence: 99%

Synthesis of Tailed Metalloporphyrins Modified with 2‐Chloronicotinic Acid and Interactions with Human Serum Albumin

Wang

Peng

Zhang

et al. 2017

Bulletin Korean Chem Soc

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Two kinds of free‐base tailed porphyrins modified with 2‐chloronicotinic acid and the corresponding Zn porphyrins have been synthesized. They have been characterized by elemental analysis and NMR, UV/Vis, fluorescence spectra, and infrared spectroscopies. Their configurations have been optimized through theoretical calculations. The fluorescence quantum yields were determined by a comparative method. The interactions between the Zn porphyrins and human serum albumin have been studied by means of fluorescence spectra. The experimental results showed that the interaction mechanism involved a combined fluorescence quenching process (static and dynamic quenching) and that the main driving force was hydrophobic in nature. Quenching constants, binding constants, thermodynamic parameters, and binding distances have been determined.

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“…With the optimised conditions in hand, the reaction of 3,8-bis-(1-bromoethyl)protoporphyrin with various alcohols was examined to investigate the generality and reaction scope ( Table 3, [4][5][6][7][8][9][10][11]. The results showed that ultrasound could markedly decrease the reaction time and the yield was significantly increased when comparing with conventional conditions.…”

mentioning

confidence: 99%

A Convenient Synthesis of Haematoporphyrin Ester-Ethers under Ultrasound Irradiation

Qiaoli

et al. 2011

Journal of Chemical Research

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The effect of porphyrin structure on binding to human serum albumin by fluorescence spectroscopy

Cited by 44 publications

References 18 publications

Molecular interaction of some cardiovascular drugs with human serum albumin at physiological‐like conditions: A new approach

Molecular interaction of some cardiovascular drugs with human serum albumin at physiological‐like conditions: A new approach

Synthesis of Tailed Metalloporphyrins Modified with 2‐Chloronicotinic Acid and Interactions with Human Serum Albumin

A Convenient Synthesis of Haematoporphyrin Ester-Ethers under Ultrasound Irradiation

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