The purification and identification of human blood serum proteins with affinity to the antitumor active RL2 lactaptin using magnetic microparticles.
RL2 antitumor agent
human blood serum proteins
identification
magnetic microparticles
mass spectrometry and western blotting
purification
Journal
Biomedical chromatography : BMC
ISSN: 1099-0801
Titre abrégé: Biomed Chromatogr
Pays: England
ID NLM: 8610241
Informations de publication
Date de publication:
Nov 2019
Nov 2019
Historique:
received:
07
05
2019
revised:
01
07
2019
accepted:
08
07
2019
pubmed:
13
7
2019
medline:
16
1
2020
entrez:
13
7
2019
Statut:
ppublish
Résumé
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.
Substances chimiques
Antineoplastic Agents
0
Blood Proteins
0
Caseins
0
Polymethacrylic Acids
0
Recombinant Proteins
0
lactaptin, human
0
polyglycidyl methacrylate
25067-05-4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e4647Subventions
Organisme : Volkswagen Shifting
ID : Grant # VW 90315
Informations de copyright
© 2019 John Wiley & Sons, Ltd.
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