A modular approach to study protein adsorption on surface modified hydroxyapatite


Autoria(s): Ozhukil Kollath, Vinayaraj; Van den Broeck, Freya; Fehér, Krisztina; Martins, José C.; Luyten, Jan; Traina, Karl; Mullens, Steven; Cloots, Rudi
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

07/12/2015

07/12/2015

2015

Resumo

Biocompatible inorganic nano- and microcarriers can be suitable candidates for protein delivery. This study demonstrates facile methods of functionalization by using nanoscale linker molecules to change the protein adsorption capacity of hydroxyapatite (HA) powder. The adsorption capacity of bovine serum albumin as a model protein has been studied with respect to the surface modifications. The selected linker molecules (lysine, arginine, and phosphoserine) can influence the adsorption capacity by changing the electrostatic nature of the HA surface. Qualitative and quantitative analyses of linker-molecule interactions with the HA surface have been performed by using NMR spectroscopy, zeta-potential measurements, X-ray photoelectron spectroscopy, and thermogravimetric analyses. Additionally, correlations to theoretical isotherm models have been calculated with respect to Langmuir and Freundlich isotherms. Lysine and arginine increased the protein adsorption, whereas phosphoserine reduced the protein adsorption. The results show that the adsorption capacity can be controlled with different functionalization, depending on the protein-carrier selections under consideration. The scientific knowledge acquired from this study can be applied in various biotechnological applications that involve biomolecule-inorganic material interfaces.

Formato

10497-10505

Identificador

http://dx.doi.org/10.1002/chem.201500223

Chemistry (weinheim an der Bergstrasse, Germany), v. 21, n. 29, p. 10497-10505, 2015.

1521-3765

http://hdl.handle.net/11449/131396

10.1002/chem.201500223

26096378

Idioma(s)

eng

Publicador

Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim

Relação

Chemistry (weinheim an der Bergstrasse, Germany)

Direitos

closedAccess

Palavras-Chave #Adsorption #Amino acids #NMR spectroscopy #Proteins #Surface chemistry
Tipo

info:eu-repo/semantics/article