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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