Adsorption of Proteins on Colloidal Lignin Particles for Advanced Biomaterials
Loading...
Access rights
openAccess
acceptedVersion
URL
Journal Title
Journal ISSN
Volume Title
A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
This publication is imported from Aalto University research portal.
View publication in the Research portal (opens in new window)
View/Open full text file from the Research portal (opens in new window)
Other link related to publication (opens in new window)
View publication in the Research portal (opens in new window)
View/Open full text file from the Research portal (opens in new window)
Other link related to publication (opens in new window)
Date
Department
Major/Subject
Mcode
Degree programme
Language
en
Pages
10
Series
Biomacromolecules, Volume 18, issue 9, pp. 2767-2776
Abstract
Coating of colloidal lignin particles (CLPs), or lignin nanoparticles (LNPs), with proteins was evaluated in order to establish a safe, self-assembly mediated modification technique to tune their surface chemistry. Gelatin and poly- l-lysine formed the most pronounced protein corona on the CLP surface, as determined by dynamic light scattering (DLS) and zeta potential measurements. Spherical morphology of individual protein coated CLPs was confirmed by transmission electron (TEM) and atomic force (AFM) microscopy. A mechanistic adsorption study with several random coiled and globular model proteins was carried out using quartz crystal microbalance with dissipation monitoring (QCM-D). The three-dimensional (3D) protein fold structure and certain amino acid interactions were decisive for the protein adsorption on the lignin surface. The main driving forces for protein adsorption were electrostatic, hydrophobic, and van der Waals interactions, and hydrogen bonding. The relative contributions of these interactions were highly dependent on the ionic strength of the surrounding medium. Capillary electrophoresis (CE) and Fourier transform infrared spectroscopy (FTIR) provided further evidence of the adsorption-enhancing role of specific amino acid residues such as serine and proline. These results have high impact on the utilization of lignin as colloidal particles in biomedicine and biodegradable materials, as the protein corona enables tailoring of the CLP surface chemistry for intended applications.Description
| openaire: EC/H2020/720303/EU//ZELCOR
Keywords
Other note
Citation
Leskinen, T, Witos, J, Valle-Delgado, J J, Lintinen, K, Kostiainen, M, Wiedmer, S K, Österberg, M & Mattinen, M L 2017, 'Adsorption of Proteins on Colloidal Lignin Particles for Advanced Biomaterials', Biomacromolecules, vol. 18, no. 9, pp. 2767-2776. https://doi.org/10.1021/acs.biomac.7b00676