• Türkçe
    • English
  • English 
    • Türkçe
    • English
  • Login
View Item 
  •   DSpace Home
  • Eczacılık Fakültesi
  • Eczacılık Teknolojisi Bölümü
  • Eczacılık Teknolojisi Bölümü Makale Koleksiyonu
  • View Item
  •   DSpace Home
  • Eczacılık Fakültesi
  • Eczacılık Teknolojisi Bölümü
  • Eczacılık Teknolojisi Bölümü Makale Koleksiyonu
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Characterization Of Protein And Peptide Binding To Nanogels Formed By Differently Charged Chitosan Derivatives

View/Open
licence.txt (265bytes)
Characterization Of Protein And Peptide Binding To Nanogels Formed By Differently Charged Chitosan Derivatives.pdf (1.913Mb)
Date
2013
Author
Zubareva, Anastasia
Ilyina, Alla
Prokhorov, Aleksander
Kurek, Denis
Efremov, Mikhail
Varlamov, Valery
Senel, Sevda
Ignatyev, Pavel
Svirshchevskaya, ?�lena
xmlui.mirage2.itemSummaryView.MetaData
Show full item record
Abstract
Chitosan (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.
URI
https://doi.org/10.3390/molecules18077848
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270036/
http://hdl.handle.net/11655/20051
xmlui.mirage2.itemSummaryView.Collections
  • Eczacılık Teknolojisi Bölümü Makale Koleksiyonu [32]
Hacettepe Üniversitesi Kütüphaneleri
Açık Erişim Birimi
Beytepe Kütüphanesi | Tel: (90 - 312) 297 6585-117 || Sağlık Bilimleri Kütüphanesi | Tel: (90 - 312) 305 1067
Bizi Takip Edebilirsiniz: Facebook | Twitter | Youtube | Instagram
Web sayfası:www.library.hacettepe.edu.tr | E-posta:openaccess@hacettepe.edu.tr
Sayfanın çıktısını almak için lütfen tıklayınız.
Contact Us | Send Feedback



DSpace software copyright © 2002-2016  DuraSpace
Theme by 
Atmire NV
 

 


DSpace@Hacettepe
huk openaire onayı
by OpenAIRE

About HUAES
Open Access PolicyGuidesSubcriptionsContact

livechat

sherpa/romeo

Browse

All of DSpaceCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsTypeDepartmentPublisherLanguageRightsIndexing SourceFundingxmlui.ArtifactBrowser.Navigation.browse_subtypeThis CollectionBy Issue DateAuthorsTitlesSubjectsTypeDepartmentPublisherLanguageRightsIndexing SourceFundingxmlui.ArtifactBrowser.Navigation.browse_subtype

My Account

LoginRegister

Statistics

View Usage Statistics

DSpace software copyright © 2002-2016  DuraSpace
Theme by 
Atmire NV