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dc.contributor.authorZubareva, Anastasia
dc.contributor.authorIlyina, Alla
dc.contributor.authorProkhorov, Aleksander
dc.contributor.authorKurek, Denis
dc.contributor.authorEfremov, Mikhail
dc.contributor.authorVarlamov, Valery
dc.contributor.authorSenel, Sevda
dc.contributor.authorIgnatyev, Pavel
dc.contributor.authorSvirshchevskaya, ?�lena
dc.date.accessioned2019-12-16T10:18:21Z
dc.date.available2019-12-16T10:18:21Z
dc.date.issued2013
dc.identifier.issn1420-3049
dc.identifier.urihttps://doi.org/10.3390/molecules18077848
dc.identifier.urihttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270036/
dc.identifier.urihttp://hdl.handle.net/11655/20051
dc.description.abstractChitosan (Chi) is a natural biodegradable cationic polymer with remarkable potency as a vehicle for drug or vaccine delivery. Chi possesses multiple groups, which can be used both for Chi derivatization and for particle formation. The aim of this work was to produce stable nanosized range Chi gels (nanogels, NGs) with different charge and to study the driving forces of complex formation between Chi NGs and proteins or peptides. Positively charged NGs of 150 nm in diameter were prepared from hexanoyl chitosan (HC) by the ionotropic gelation method while negatively charged NGs of 190 nm were obtained from succinoyl Chi (SC) by a Ca2+ coacervation approach. NGs were loaded with a panel of proteins or peptides with different weights and charges. We show that NGs preferentially formed complexes with oppositely charged molecules, especially peptides, as was demonstrated by gel-electrophoresis, confocal microscopy and HPLC. Complex formation was accompanied by a change in zeta-potential and decrease in size. We concluded that complex formation between Chi NGs and peptide/proteins is mediated mostly by electrostatic interactions.
dc.relation.isversionof10.3390/molecules18077848
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleCharacterization Of Protein And Peptide Binding To Nanogels Formed By Differently Charged Chitosan Derivatives
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:eu-repo/semantics/publishedVersion
dc.relation.journalMolecules
dc.contributor.departmentFarmasötik Teknoloji
dc.identifier.volume18
dc.identifier.issue7
dc.identifier.startpage7848
dc.identifier.endpage7864
dc.description.indexPubMed
dc.description.indexWoS
dc.description.indexScopus


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