The purification and identification of human blood serum proteins with affinity to the antitumor active RL2 lactaptin using magnetic microparticles

0509686 - ÚMCH 2020 RIV GB eng J - Journal Article
Manko, N. - Starykovych, M. - Bobak, Y. - Stoika, R. - Richter, V. - Koval, O. - Lavrik, I. - Horák, Daniel - Souchelnytskyi, S. - Kit, Y.
The purification and identification of human blood serum proteins with affinity to the antitumor active RL2 lactaptin using magnetic microparticles.
Biomedical Chromatography. Roč. 33, č. 11 (2019), s. 1-6, č. článku e4647. ISSN 0269-3879. E-ISSN 1099-0801
Institutional support: RVO:61389013
Keywords : human blood serum proteins * dentification * magnetic microparticles
OECD category: Polymer science
Impact factor: 1.728, year: 2019
Method of publishing: Limited access
https://onlinelibrary.wiley.com/doi/full/10.1002/bmc.4647

The cytopoxic effect of RL2 lactaptin (the recombinant analog of proteolytic fragment of human kappa‐casein) toward tumor cells in vitro and in vivo presents it as a novel promising antitumor drug. The binding of any drug with serum proteins can affect their activity, distribution, rate of excretion and toxicity in the human body. Here, we studied the ability of RL2 to bind to various blood serum proteins. Using magnetic microparticles bearing by RL2 as an affinity matrix, in combination with mass spectrometry and western blot analysis, we found a number of blood serum proteins possessing affinity for RL2. Among them IgA, IgM and IgG subclasses of immunoglobulins, apolipoprotein A1 and various cortactin isoforms were identified. This data suggests that in the bloodstream RL2 lactaptin takes part in complicate protein–protein interactions, which can affect its activity.
Permanent Link: http://hdl.handle.net/11104/0300605