Pandey Gunjan, Fatma Tasneem, Komath Sneha Sudha
School of Biosciences, Jamia Millia Islamia, New Delhi, India.
Photochem Photobiol. 2009 Sep-Oct;85(5):1126-33. doi: 10.1111/j.1751-1097.2009.00571.x. Epub 2009 May 28.
In a recent study, we found that jacalin, a T-antigen specific lectin could interact with phycocyanin (PC) in a carbohydrate-independent manner. We show here that concanavalin A and peanut agglutinin too can interact with PC, although the nature of the interaction is distinctly different from that for jacalin. The legume lectins bind PC weaker in the presence of their specific carbohydrate ligands. Like jacalin, the legume lectins too interact with PC via two distinct sites. Higher ionic strengths resulted in a weakening of the interaction at site 1 and did not affect the interaction at site 2, clearly indicating that the interactions involve charged residues at the former and hydrophobic interactions at the latter site. The implications for the use of these lectin-PC complexes in photodynamic therapy and other clinical applications are discussed.
在最近的一项研究中，我们发现，一种T抗原特异性凝集素——红豆蔻凝集素（jacalin）能够以不依赖碳水化合物的方式与藻蓝蛋白（PC）相互作用。我们在此表明，伴刀豆球蛋白A和花生凝集素也能与PC相互作用，尽管其相互作用的性质与红豆蔻凝集素的明显不同。在其特异性碳水化合物配体存在的情况下，豆类凝集素与PC的结合较弱。与红豆蔻凝集素一样，豆类凝集素也通过两个不同的位点与PC相互作用。较高的离子强度导致位点1处的相互作用减弱，而不影响位点2处的相互作用，这清楚地表明，前者的相互作用涉及带电残基，而后者的相互作用涉及疏水相互作用。本文讨论了这些凝集素-PC复合物在光动力疗法和其他临床应用中的潜在用途。
