Functional Equality in the Absence of Structural Similarity

Goel, Manisha; Jain, Deepti; Kaur, Kanwal J.; Kenoth, Roopa; Maiya, Bhaskar G.; Swamy, Musti J.; Salunke, Dinakar M.

doi:10.1074/jbc.m105387200

Cited by 42 publications

(53 citation statements)

References 39 publications

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“…The binding appears to be predominantly through hydrophobic interactions as both cationic and anionic porphyrins were bound. Similar results were found for Jacalin, which recognizes the tumor associated T-antigenic structure Galβ13GalNAc and could bind one porphyrin [89] . Another example is the interaction of water soluble freebase and metalloporphyrins (639a/b, 640a/b, 641a and 74) with Momordica charantia (bitter gourd) lectin (MCL), a tetrameric galactose-specific glycoprotein.…”

Section: Lectin Bindingsupporting

confidence: 73%

“…Similar to interactions with glycoproteins, porphyrins have been shown to exhibit other physiological interactions with, for example, lectins, i.e., specific carbohydrate recognition proteins. Several examples exist of metalloporphyrins binding to plant lectins where the association constant (K a ) and stoichiometry of binding have been determined [87][88][89] . In most cases the addition of the binding sugar appears to have no effect on the binding of the porphyrin, i.e., their binding sites are different.…”

Section: Porphyrin Bioconjugatesmentioning

confidence: 99%

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Chemical Synthesis and Medicinal Applications of Glycoporphyrins

Moylan¹,

Scanlan²,

Senge

2015

CMC

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Abstract:This review presents an in-depth overview of the modification of porphyrins with bioconjugates and their applications in medicine today. Porphyrin bioconjugates ranging from nucleotides to steroids are under active scrutiny. However, carbohydrates have been at the forefront of such research in recent years and offer significant potential. This is attributed to their own selectivity to lectins on the surface of cancer cells and their influence on the amphiphilicity of the porphyrin macrocycle. These characteristics and the tendency of porphyrin photosensitizers to accumulate in tumor tissues make glycoporphyrins promising candidates for use as photosensitizers. Thus, a detailed overview of the synthesis and biological evaluation of glycoporphyrins is given with a particular focus on their applications in photodynamic therapy and their future prospects as drug candidates have been reported.

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Section: Lectin Bindingsupporting

confidence: 73%

Section: Porphyrin Bioconjugatesmentioning

confidence: 99%

Chemical Synthesis and Medicinal Applications of Glycoporphyrins

Moylan¹,

Scanlan²,

Senge

2015

CMC

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“…The thermodynamic parameters (DH8 and DS8) obtained for pea lectin-porphyrin interaction (Table 1) suggest that (20).…”

Section: Discussionmentioning

confidence: 99%

“…Enthalpy-entropy compensation has been attributed to the solvent reorganization during binding process (46). In this context, it is interesting to note that in the crystal structure of Con A-H 2 TSPP complex, binding of H 2 TSPP to Con A is mediated by hydrogen bonds with bridging water molecules in between (20). It is possible that porphyrin binding to pea lectin may be similar to the binding of porphyrins to Con A and involve water molecules in the overall binding process.…”

Section: Discussionmentioning

confidence: 99%

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Thermodynamic studies on the interaction of water-soluble porphyrins with the glucose/mannose-specific lectin from garden pea (Pisum sativum)

Kavitha

Swamy

2006

TBMB

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SummaryDue to the application of porphyrins as photosensitizers in photodynamic therapy to treat cancer, and the ability of some lectins to preferentially recognize tumor cells, studies on the interaction of porphyrins with lectins are of considerable interest. Here we report thermodynamic studies on the interaction of several free-base and metallo-porphyrins with pea (Pisum sativum) lectin (PSL). Association constants (K a ) were obtained by absorption titrations by monitoring changes in the Soret band of the porphyrins and the K a values obtained for various porphyrins at different temperatures are in the range of 1.0 6 10 4 to 8.0 6 10 4 M 71 . Both cationic and anionic porphyrins were found to bind to PSL with comparable affinity. Presence of 0.1 M methyl-a-D-mannopyranoside -a carbohydrate ligand that is specifically recognised by PSLdid not affect the binding significantly, suggesting that porphyrin and sugar bind at different sites on the lectin. From the temperature dependence of the K a values, the thermodynamic parameters, change in enthalpy and change in entropy associated with the binding process were estimated. These values were found to be in the range: DH8 ¼ 795.4 to 733.9 kJ Á mol 71 and DS8 ¼ 7237.2 to 732.2 J Á mol 71 Á K 71 , indicating that porphyrin binding to pea lectin is driven largely by enthalpic forces with the entropic contribution being negative. Enthalpy-entropy compensation was observed in the interaction of different porphyrins to PSL, with the exception of meso-tetra-(4-sulfonatophenyl)porphyrinato zinc(II), emphasizing the role of water structure in the overall binding process. Circular dichroism and differential scanning calorimetric studies indicate that while porphyrin binding does not induce significant changes in the lectin structure and thermal stability, carbohydrate binding induces moderate changes in the tertiary structure of the protein and also increases its thermal unfolding temperature and the enthalpy of the unfolding transition.IUBMB Life, 58: 720-730, 2006

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Protein Dimerization on a Phosphonated Calix[6]arene Disc

et al. 2017

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Complex formation between cationic cytochrome c and the water‐soluble, poly‐anionic p‐phosphonatocalix[6]arene (pclx6) was investigated. A crystal structure (at 1.8 Å resolution) revealed a remarkable dimeric disc of pclx6 that acts like glue to mediate a symmetric (C2) protein dimer. The calixarene disc has a diameter of about 1.5 nm and masks about 360 Å2 of protein surface. The key protein–calixarene contacts occur via two linchpin lysines, with additional contacts provided by a small hydrophobic patch. The protein–calixarene supramolecular assemblies were observed in solution by size‐exclusion chromatography with multi‐angle light scattering and NMR spectroscopy. Using isothermal titration calorimetry and NMR data, an apparent Kd in the low micromolar range was determined for the charge‐rich protein–calixarene complex. In contrast to p‐sulfonatocalix[4]arene, the larger pclx6 has a single, well‐defined binding site that mediates the assembly of cytochrome c in solution.

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Functional Equality in the Absence of Structural Similarity

Abstract: The crystal structure of meso-tetrasulfonatophenylporphyrin complexed with concanavalin A (ConA) was determined at 1.9 Å resolution.

Cited by 42 publications

References 39 publications

Chemical Synthesis and Medicinal Applications of Glycoporphyrins

Chemical Synthesis and Medicinal Applications of Glycoporphyrins

Thermodynamic studies on the interaction of water-soluble porphyrins with the glucose/mannose-specific lectin from garden pea (Pisum sativum)

Protein Dimerization on a Phosphonated Calix[6]arene Disc

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