Você está no menu de acessibilidade

Utilize este identificador para citar ou criar um link para este item: http://acervodigital.unesp.br/handle/11449/131396
Título: 
A modular approach to study protein adsorption on surface modified hydroxyapatite
Autor(es): 
Instituição: 
  • University of Liège
  • Flemish Institute for Technological Research (VITO)
  • Ghent University
  • Katholieke Universiteit Leuven
  • Universidade Estadual Paulista (UNESP)
ISSN: 
1521-3765
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.
Data de publicação: 
2015
Citação: 
Chemistry (weinheim an der Bergstrasse, Germany), v. 21, n. 29, p. 10497-10505, 2015.
Duração: 
10497-10505
Publicador: 
Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
Palavras-chaves: 
  • Adsorption
  • Amino acids
  • NMR spectroscopy
  • Proteins
  • Surface chemistry
Fonte: 
http://dx.doi.org/10.1002/chem.201500223
Endereço permanente: 
Direitos de acesso: 
Acesso restrito
Tipo: 
outro
Fonte completa:
http://repositorio.unesp.br/handle/11449/131396
Aparece nas coleções:Artigos, TCCs, Teses e Dissertações da Unesp

Não há nenhum arquivo associado com este item.
 

Itens do Acervo digital da UNESP são protegidos por direitos autorais reservados a menos que seja expresso o contrário.