Adsorption of Proteins on Colloidal Lignin Particles for Advanced Biomaterials

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Adsorption of Proteins on Colloidal Lignin Particles for Advanced Biomaterials. / Leskinen, Timo; Witos, Joanna; Valle-Delgado, Juan José; Lintinen, Kalle; Kostiainen, Mauri; Wiedmer, Susanne K.; Österberg, Monika; Mattinen, Maija Liisa.

julkaisussa: Biomacromolecules, Vuosikerta 18, Nro 9, 11.09.2017, s. 2767-2776.

Tutkimustuotos: Lehtiartikkelivertaisarvioitu

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Bibtex - Lataa

@article{dd327795d2e342af8715b66058249df8,
title = "Adsorption of Proteins on Colloidal Lignin Particles for Advanced Biomaterials",
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.",
author = "Timo Leskinen and Joanna Witos and Valle-Delgado, {Juan Jos{\'e}} and Kalle Lintinen and Mauri Kostiainen and Wiedmer, {Susanne K.} and Monika {\"O}sterberg and Mattinen, {Maija Liisa}",
note = "| openaire: EC/H2020/720303/EU//ZELCOR",
year = "2017",
month = "9",
day = "11",
doi = "10.1021/acs.biomac.7b00676",
language = "English",
volume = "18",
pages = "2767--2776",
journal = "Biomacromolecules",
issn = "1525-7797",
publisher = "AMERICAN CHEMICAL SOCIETY",
number = "9",

}

RIS - Lataa

TY - JOUR

T1 - Adsorption of Proteins on Colloidal Lignin Particles for Advanced Biomaterials

AU - Leskinen, Timo

AU - Witos, Joanna

AU - Valle-Delgado, Juan José

AU - Lintinen, Kalle

AU - Kostiainen, Mauri

AU - Wiedmer, Susanne K.

AU - Österberg, Monika

AU - Mattinen, Maija Liisa

N1 - | openaire: EC/H2020/720303/EU//ZELCOR

PY - 2017/9/11

Y1 - 2017/9/11

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85029223642&partnerID=8YFLogxK

U2 - 10.1021/acs.biomac.7b00676

DO - 10.1021/acs.biomac.7b00676

M3 - Article

VL - 18

SP - 2767

EP - 2776

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 9

ER -

ID: 15681496