Photooxidation of lysozyme or serum albumin bound to meso-tetra-arylporphyrins

Zhang, Yazhou; Görner, Helmut

doi:10.1016/j.dyepig.2010.10.011

Cited by 6 publications

(2 citation statements)

References 46 publications

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“…As a proof of concept of the feasibility of utilizing Star3600_Hg for the degradation of proteins containing l -Trp residues, the interaction of Star3600_Hg with lysozyme in aqueous solution (5 µM) was investigated. Lysozyme (LSZ) is a well-known protein, with an average molecular weight of about 14.6 kDa, and six tryptophane residues on its structure [ 54 ].…”

Section: Resultsmentioning

confidence: 99%

Water-Soluble Star Polymer as a Potential Photoactivated Nanotool for Lysozyme Degradation

Mezzina,

Nicosia,

Barone

et al. 2024

Polymers

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The development of nanotools for chemical sensing and macromolecular modifications is a new challenge in the biomedical field, with emphasis on artificial peptidases designed to cleave peptide bonds at specific sites. In this landscape, metal porphyrins are attractive due to their ability to form stable complexes with amino acids and to generate reactive oxygen species when irradiated by light of appropriate wavelengths. The issues of hydrophobic behavior and aggregation in aqueous environments of porphyrins can be solved by using its PEGylated derivatives. This work proposes the design of an artificial photo-protease agent based on a PEGylated mercury porphyrin, able to form a stable complex with l-Tryptophan, an amino acid present also in the lysozyme structure (a well-known protein model). The sensing and photodegradation features of PEGylated mercury porphyrin were exploited to detect and degrade both l-Trp and lysozyme using ROS, generated under green (532 nm) and red (650 nm) light lasers. The obtained system (Star3600_Hg) and its behavior as a photo-protease agent were studied by means of several spectroscopies (UV-Vis, fluorescence and circular dichroism), and MALDI-TOF mass spectrometry, showing the cleavage of lysozyme and the appearance of several short-chain residues. The approach of this study paves the way for potential applications in theranostics and targeted bio-medical therapies.

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Section: Resultsmentioning

confidence: 99%

Water-Soluble Star Polymer as a Potential Photoactivated Nanotool for Lysozyme Degradation

Mezzina,

Nicosia,

Barone

et al. 2024

Polymers

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“…The research on water-soluble porphyrins has received much interest in recent years [1][2][3][4][5][6]. Because of their excellent bioactivity water-soluble cationic porphyrins can be used as potential anticancer [7,8], antibacterial agents [9,10] and probe for structure and dynamics of DNA [11].…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic Studies on the Interaction of a Water-Soluble Cationic Porphyrin with Bovine Serum Albumin

Dezhampanah

Bordbar

Khodadusdt

2013

Analytical Cellular Pathology

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The interaction of a water-soluble cationic porphyrin, Cobalt(III) 5, 10, 15, 20-tetrakis (1-methylpyridinium-4-yl) porphyrin [Co(III)TMPyP], with bovine serum albumin (BSA) has been studied in 1 mM phosphate buffer pH 7.0 containing 5 mM NaCl by UV-vis absorption, resonance light scattering (RLS) and fluorescence spectroscopies at 25°C. The results of RLS studies represent no aggregate formation of porphyrin in the surface of BSA and low tendency of this porphyrin for aggregate formation.The binding of porphyrin complex to BSA quenches fluorescence emission of BSA via a dynamic mechanism and the quenching process obeys a linear Stern-Volmer relationship. The values of Stern-Volmer constants, KSV, was determined nearly 105 M−1, that depend on BSA concentration. The average aggregation number of BSA calculated from the analysis of fluorescence quenching data indicates that absence of any porphyrin induced aggregation of BSA due to its interaction with porphyrin complex. The binding of Co(III) TMPyP had no obvious effect on the molecular conformation of the protein. Electrostatic force played an important role in the binding due to the opposite charges on porphyrin and the protein.

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Photoprocesses of merocyanine 540 bound to serum albumin and lysozyme

Zhang

Görner

2012

Journal of Molecular Structure

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Photooxidation of lysozyme or serum albumin bound to meso-tetra-arylporphyrins

Cited by 6 publications

References 46 publications

Water-Soluble Star Polymer as a Potential Photoactivated Nanotool for Lysozyme Degradation

Water-Soluble Star Polymer as a Potential Photoactivated Nanotool for Lysozyme Degradation

Spectroscopic Studies on the Interaction of a Water-Soluble Cationic Porphyrin with Bovine Serum Albumin

Photoprocesses of merocyanine 540 bound to serum albumin and lysozyme

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