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

V. O. Shipunova, M. P. Nikitin, I. V. Zelepukin, P. I. Nikitin, S. M. Deyev, R. V. Petrov

Research output: Contribution to journalArticle

5 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)315-318
Number of pages4
JournalDoklady Biochemistry and Biophysics
Volume464
Issue number1
DOIs
Publication statusPublished - 1 Sep 2015
Externally publishedYes

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Lectins
Glycoproteins
Nanoparticles
Glycosylation
Proteins
Monosaccharides
Chemical analysis
Theranostic Nanomedicine
Therapeutics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Chemistry(all)

Cite this

A comprehensive study of interactions between lectins and glycoproteins for the development of effective theranostic nanoagents. / Shipunova, V. O.; Nikitin, M. P.; Zelepukin, I. V.; Nikitin, P. I.; Deyev, S. M.; Petrov, R. V.

In: Doklady Biochemistry and Biophysics, Vol. 464, No. 1, 01.09.2015, p. 315-318.

Research output: Contribution to journalArticle

Shipunova, V. O. ; Nikitin, M. P. ; Zelepukin, I. V. ; Nikitin, P. I. ; Deyev, S. M. ; Petrov, R. V. / A comprehensive study of interactions between lectins and glycoproteins for the development of effective theranostic nanoagents. In: Doklady Biochemistry and Biophysics. 2015 ; Vol. 464, No. 1. pp. 315-318.
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