Synthesis of di(glucosyloxo)phosphorus tetraphenylporphyrin complex with affinity to glucose-binding concanavalin A. (September 2015)

• Record Type: Journal Article
• Authors: Matsumoto, Jin; Sato, Shunsuke; Shiragami, Tsutomu; Yasuda, Masahide
• Is Part Of: Dyes and pigments. Volume 120(2015)
• Page Start: 147
• Page End: 154
• Publication Date: 2015-09
• Subjects: Water-soluble porphyrin -- Axial ligand -- Glycosyl ligand -- Lectin -- Photosensitizer -- Photodynamic therapy; Dyes and dyeing -- Periodicals; Pigments -- Periodicals; 667.2
• DOI: 10.1016/j.dyepig.2015.04.011
• Languages: English
• ISSNs: 0143-7208

Abstract

Abstract: A new di(glucopyranosyloxo)phosphorus tetraphenylporphyrin complex containing axial acetylated glucosyl ligands (1a ) and its deacetylated derivative (1b ) were synthesized. The bio-affinity of1 to the lectin concanavalin A (ConA) was evaluated by various spectroscopic analyses. Both1a and1b were bound to ConA because the fluorescence of ConA arising from tryptophan and tyrosine residues was statically quenched by1 . Their absorption spectra also shifted to longer wavelengths upon ConA addition. These spectral changes provided binding constants of 4.5 × 10 4 and 6.4 × 10 4 M −1 for1a and1b, respectively. Moreover, ConA efficiently quenched the fluorescence of1a but not that of1b . This result demonstrated that1b was site-specifically bound to a glucose binding site comprising the tyrosine residues, albeit far from tryptophan residues. On the other hand, 1a adsorbed less specifically on the entire ConA protein. Highlights: Phosphorus porphyrin complex containing axial glucosyl ligands was synthesized. The bio-affinity to lectin concanavalin A (ConA) was evaluated spectroscopically. The complex was site-specifically bound to the glucose-binding site of ConA.