The purification and identification of human blood serum proteins with affinity to the antitumor active RL2 lactaptin using magnetic microparticles. (18th August 2019)

• Record Type: Journal Article
• Authors: Manko, Nazar; Starykovych, Marina; Bobak, Yaroslav; Stoika, Rostyslav; Richter, Vladimir; Koval, Olga; Lavrik, Inna; Horák, Daniel; Souchelnytskyi, Serhiy; Kit, Yuriy
• Is Part Of: Biomedical chromatography. Volume 33:Number 11(2019)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2019-08-18
• Subjects: human blood serum proteins -- identification -- magnetic microparticles -- mass spectrometry and western blotting -- purification -- RL2 antitumor agent; Chromatographic analysis -- Periodicals; Biology -- Periodicals; Medicine -- Periodicals; Biology -- Periodicals; Chromatography -- methods -- Periodicals; Medicine -- Periodicals; 543.089
• DOI: 10.1002/bmc.4647
• Languages: English
• ISSNs: 0269-3879

Abstract

Abstract: 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.