2011
DOI: 10.5504/bbeq.2011.0057
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Interaction of Wheat Germ Agglutinin with Porphyrin Compounds—Potential Anticancer Agents

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Cited by 7 publications
(2 citation statements)
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“…The curve revealed cooperative interactions which indicated that binding of one FeTMPyP molecule facilitated the interaction of the next FeTMPyP molecules by enhancing the affinity of the vacant binding sites on the lectin. The obtained results demonstrated that the legume lectin Con A bound FeTMPyP with high affinity, similar to that of the non-legume lectin WGA for iron porphyrins [ 18 , 19 ].…”
Section: Resultsmentioning
confidence: 83%
“…The curve revealed cooperative interactions which indicated that binding of one FeTMPyP molecule facilitated the interaction of the next FeTMPyP molecules by enhancing the affinity of the vacant binding sites on the lectin. The obtained results demonstrated that the legume lectin Con A bound FeTMPyP with high affinity, similar to that of the non-legume lectin WGA for iron porphyrins [ 18 , 19 ].…”
Section: Resultsmentioning
confidence: 83%
“…Recently, T/Tn specific lectins have been identified as potential targeting molecules [29]. The non-covalent binding of porphyrins to lectins was well studied [30, Bogoeva, 2010 #314], particularly the interaction of wheat germ agglutinin (WGA) [31][32][33][34] and Con A with porphyrins was evaluated and affinity constants in micromolar range were calculated, accordingly [35,36].…”
Section: Why Lectins Are Useful Tools For the Targeted Therapy?mentioning
confidence: 99%