Assessment of new cationic porphyrin binding to plasma proteins by planar microarray and spectroscopic methods

Porphyrins have a unique aromatic structure determining particular photochemical properties that make them promising photosensitizers for anticancer therapy. Previously, we synthesized a set of artificial porphyrins by modifying side-chain functional groups and introducing different metals into the...

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Bibliographic Details
Published in:Journal of biomolecular structure & dynamics Vol. 31; no. 4; pp. 363 - 375
Main Authors: Gyulkhandanyan, Aram, Gyulkhandanyan, Lusine, Ghazaryan, Robert, Fleury, Fabrice, Angelini, Marie, Gyulkhandanyan, Grigor, Sakanyan, Vehary
Format: Journal Article
Language:English
Published: England Routledge 01.04.2013
Subjects:
Animals
Binding, Competitive - drug effects
Blood Proteins - chemistry
Blood Proteins - metabolism
cationic porphyrins
Cations
Cattle
competition assays
Computer Simulation
Hemoglobins - chemistry
Hemoglobins - metabolism
Humans
Kinetics
long-chain fatty acids
microarrays
Models, Molecular
Molecular Conformation
Palmitic Acids - metabolism
Palmitic Acids - pharmacology
plasma proteins
Porphyrins - chemistry
Porphyrins - metabolism
Protein Array Analysis - methods
Protein Binding - drug effects
Protein Conformation
Protein Structure, Tertiary
Serum Albumin - chemistry
Serum Albumin - metabolism
Serum Albumin, Bovine - chemistry
Serum Albumin, Bovine - metabolism
Spectroscopy, Near-Infrared - methods
Stearic Acids - metabolism
Stearic Acids - pharmacology
ISSN:0739-1102, 1538-0254, 1538-0254
Online Access:Get full text
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Summary:Porphyrins have a unique aromatic structure determining particular photochemical properties that make them promising photosensitizers for anticancer therapy. Previously, we synthesized a set of artificial porphyrins by modifying side-chain functional groups and introducing different metals into the core structure. Here, we have performed a comparative study of the binding properties of 29 cationic porphyrins with plasma proteins by using microarray and spectroscopic approaches. The porphyrins were noncovalently immobilized onto hydrogel-covered glass slides and probed to bio-conjugated human and bovine serum albumins, as well as to human hemoglobin. The signal detection was carried out at the near-infrared fluorescence wavelength (800 nm) that enabled the effect of intrinsic visible wavelength fluorescence emitted by the porphyrins tested to be discarded. Competition assays on porphyrin microarrays indicated that long-chain fatty acids (FAs) (palmitic and stearic acids) decrease porphyrin binding to both serum albumin and hemoglobin. The binding affinity of different types of cationic porphyrins for plasma proteins was quantitatively assessed in the absence and presence of FAs by fluorescent and absorption spectroscopy. Molecular docking analysis confirmed results that new porphyrins and long-chain FAs compete for the common binding site FA1 in human serum albumin and meso-substituted functional groups in porphyrins play major role in the modulation of conformational rearrangements of the protein.
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ISSN:0739-1102
1538-0254
1538-0254
DOI:10.1080/07391102.2012.703063