A comprehensive study of interactions between lectins and glycoproteins for the development of effective theranostic nanoagents.

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Abstract

A comprehensive study of the interactions between lectins and glycoproteins possessing different glycosylation profiles in the composition of nanoparticles was carried out in order to find specifically interacting protein pairs for the creation of novel classes of multifunctional nanoagets that based on protein-assisted selfassembly. We obtained information about specific interactions of certain lectins with selected glycoproteins as well as about the ability of certain monosaccharides to competitively inhibit binding of glycoproteins with lectins. These protein-mediated interactions may be involved in the formulation of self-assembled nanoparticles for therapy and diagnostics of various diseases.

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Journal

Journal ID (iso-abbrev): Dokl Biochem Biophys

Title: Doklady. Biochemistry and biophysics

Publisher: Pleiades Publishing Ltd

ISSN (Electronic): 1608-3091

ISSN (Print): 1607-6729

Publication date (Electronic): 2015

Volume: 464

Affiliations

[1 ] Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia. viktoriya.shipunova@phystech.edu.

[2 ] Nizhny Novgorod State University, pr. Gagarina 23, Nizhny Novgorod, 603600, Russia. viktoriya.shipunova@phystech.edu.

[3 ] Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia.

[4 ] Moscow Institute of Physics and Technology (State University), Institutskii per. 9, Dolgoprudnyi, Moscow oblast, 141700, Russia.

[5 ] Prokhorov Institute of General Physics, Russian Academy of Sciences, ul. Vavilova 38, Moscow, 119991, Russia.

[6 ] National Research Nuclear University "Moscow Engineering Physics Institute,", Moscow, Russia.

[7 ] Nizhny Novgorod State University, pr. Gagarina 23, Nizhny Novgorod, 603600, Russia.

Article

Publisher Item ID: 10.1134/S1607672915050117

DOI: 10.1134/S1607672915050117

PubMed ID: 26518557

SO-VID: 88fc49f6-bda0-44ce-8c3d-9c1538ca992f

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