Biopolym. Cell. 2026; 42(3):163-170.
https://doi.org/10.7124/bc.000BB7
Structure and Function of Biopolymers
Domain-specific binding of lactoferrin to plasminogen fragments
1Kapustianenko L. G., 1Yusova O. I., 1Korsa V. V., 1Tykhomyrov A. O.
  1. Palladin Institute of Biochemistry, NAS of Ukraine
    9, Leontovicha str., Kyiv, Ukraine, 01054

Abstract

Aim. The aim of the study was to determine affinity of lactoferrin binding to Glu-plasminogen (Glu-Pg) and its fragments: kringles 1-3, 4 and 5 (K1-3, K4 and K5), and Val442-plasminogen (mini-Pg) in order to reveal plausible lactoferrin influence on the plasminogen/plasmin system. Methods. Glu-Pg, K1-3, K4, K5, and mini-Pg were tested for their ability to bind lactoferrin by ELISA using polyclonal antibodies to lactoferrin. Additionally, complex formation between lactoferrin and K4, K5 and mini-Pg was confirmed by Far-western blotting technique. Results. We demonstrated lactoferrin binding to Glu-Pg, K1-3, K4, K5, and mini-Pg in a concentration-dependent manner. The calculated dissociation constants range from 1.06 × 10-7 M to 7.29 × 10-8 M, indicating a strong interaction between tested Glu-Pg domains and lactoferrin. Overall, lactoferrin exhibits the strongest affinity for K5, suggesting a potential preferential binding site within the whole plasminogen molecule. Conclusions. The obtained data support a potential previously reported inhibitory role of lactoferrin in the plasminogen/plasmin system.
Keywords: plasminogen/plasmin system, kringles, lactoferrin, protein-protein interactions, ELISA
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