Interactions of bioactive molecules with thin dendritic glycopolymer layers

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Eva Bittrich - , Leibniz Institute of Polymer Research Dresden (Author)
  • Flavia Mele - , Turin Polytechnic University in Tashkent, Leibniz Institute of Polymer Research Dresden (Author)
  • Andreas Janke - , Leibniz Institute of Polymer Research Dresden (Author)
  • Frank Simon - , Leibniz Institute of Polymer Research Dresden (Author)
  • Klaus-Jochen Eichhorn - , Leibniz Institute of Polymer Research Dresden (Author)
  • Brigitte Voit - , Chair of Organic Chemistry of Polymers, Leibniz Institute of Polymer Research Dresden, TUD Dresden University of Technology (Author)
  • Dietmar Appelhans - , Leibniz Institute of Polymer Research Dresden (Author)

Abstract

The authors report on highly swellable, stable layers of spherical dendritic glycopolymers, composed of hyperbranched poly(ethylene imine) (PEI) as core and two different maltose shells (A = dense shell and B = open shell). These glycopolymers are cross-linked and attached with poly(ethylene-alt-maleic anhydride) (PEMA) or citric acid on SiOx substrates. The swelling and adsorption of biomolecules were analyzed by spectroscopic ellipsometry and quartz crystal microbalance with dissipation. The swelling degree and complexation with the drug molecule adenosine triphosphate (ATP) were found to be up to 10 times higher for dendritic glycopolymer layers cross-linked with PEMA than for layers cross-linked with citric acid. ATP complexation by electrostatic interaction with the PEI cores was confirmed by x-ray photoelectron spectroscopy analysis. Complexation led to partial collapsing, stiffening, and increase of polymer layer viscosity of the PEMA cross-linked layers. From modeling of ellipsometric data, it was deduced that ATP complexation preferably takes place at the polymer layer-solution interface. The size effect of the adsorbates was investigated by comparing ATP complexation with the adsorption of larger vitamin B12 and human serum albumin (HSA) protein. PEI-Mal A cross-linked with PEMA was found to be resistant toward B12 and HSA adsorption due to the diffusion barrier of the polymer layer. Thus, the authors present potentially biocompatible polymer surfaces for drug loading and their surface supported release. Published by the AVS.

Details

Original languageGerman
Number of pages15
JournalBiointerphases
Volume13
Issue number6
Publication statusPublished - 2018
Peer-reviewedYes

External IDs

PubMed 30227717
Scopus 85053735503
ORCID /0000-0002-4531-691X/work/148608060

Keywords

Keywords

  • Quartz-crystal microbalance, Human-serum-albumin, Pvfa-co-pvam, Poly(ethylene imine), Protein adsorption, Polyelectrolyte multilayers, Polymer capsules, Drug-delivery, Poly(propyleneimine) dendrimers, Polyamidoamine dendrimers