Relevant Properties for Immobilizing Short Peptides on Biosurfaces

P. Sevilla; J. Gil; C. Aparicio

doi:10.1016/j.irbm.2017.06.003

Relevant Properties for Immobilizing Short Peptides on Biosurfaces

P. Sevilla, J. Gil, C. Aparicio

Biomaterials

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Understanding protein and oligopeptide adsorption on biomaterial surfaces is important to develop new biomaterials with improved properties. The phenomenon of peptide adsorption is determined by many parameters such environmental pH, surface topographical features, surface polarity, peptide structure, and/or surface and peptide electric charges. We assessed the effect of surface and peptide net charges on oligopeptide adsorption on synthetic surfaces under different conditions. We have also assessed the ability of immobilizing peptides on the surface generating covalent bonds or electrostatic attraction. Direct relation between the amount of peptide adsorbed on the surface and the difference in net charge between surface and peptides was determined. No relation between the difference in net charge and the ability to promote covalent bonds between peptide and surface was found. Competitive adsorption experiments confirmed these findings. Understanding the specific interactions during adsorption of peptides onto synthetic surfaces improves our ability to develop strategies for the efficient immobilization of oligopeptides on biomaterial surfaces.

Original language	English (US)
Pages (from-to)	256-265
Number of pages	10
Journal	IRBM
Volume	38
Issue number	5
DOIs	https://doi.org/10.1016/j.irbm.2017.06.003
State	Published - Oct 2017

Bibliographical note

Funding Information:
This work was partially supported by the University of Minnesota through a Grant-in-Aid of Research, Artistry, and Scholarly (CA), and the Spanish Ministry of Economy and Competitiveness (project MAT 2012-30706) (FJG). PS acknowledges financial support from the Spanish Ministry of Economy and Competitiveness through a fellowship for research stays at international institutions (FPU-MEC). Parts of this work were carried out in the University of Minnesota I.T. Characterization Facility, which receives partial support from NSF through the MRSEC program. Parts of this work were carried out in the Institute for Bioengineering of Catalonia-IBEC.

Publisher Copyright:
© 2017 AGBM

Keywords

Adsorption
Biofunctionalization
Peptide
Silanization
Surface charge
Titanium

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abstract = "Understanding protein and oligopeptide adsorption on biomaterial surfaces is important to develop new biomaterials with improved properties. The phenomenon of peptide adsorption is determined by many parameters such environmental pH, surface topographical features, surface polarity, peptide structure, and/or surface and peptide electric charges. We assessed the effect of surface and peptide net charges on oligopeptide adsorption on synthetic surfaces under different conditions. We have also assessed the ability of immobilizing peptides on the surface generating covalent bonds or electrostatic attraction. Direct relation between the amount of peptide adsorbed on the surface and the difference in net charge between surface and peptides was determined. No relation between the difference in net charge and the ability to promote covalent bonds between peptide and surface was found. Competitive adsorption experiments confirmed these findings. Understanding the specific interactions during adsorption of peptides onto synthetic surfaces improves our ability to develop strategies for the efficient immobilization of oligopeptides on biomaterial surfaces.",

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N2 - Understanding protein and oligopeptide adsorption on biomaterial surfaces is important to develop new biomaterials with improved properties. The phenomenon of peptide adsorption is determined by many parameters such environmental pH, surface topographical features, surface polarity, peptide structure, and/or surface and peptide electric charges. We assessed the effect of surface and peptide net charges on oligopeptide adsorption on synthetic surfaces under different conditions. We have also assessed the ability of immobilizing peptides on the surface generating covalent bonds or electrostatic attraction. Direct relation between the amount of peptide adsorbed on the surface and the difference in net charge between surface and peptides was determined. No relation between the difference in net charge and the ability to promote covalent bonds between peptide and surface was found. Competitive adsorption experiments confirmed these findings. Understanding the specific interactions during adsorption of peptides onto synthetic surfaces improves our ability to develop strategies for the efficient immobilization of oligopeptides on biomaterial surfaces.

AB - Understanding protein and oligopeptide adsorption on biomaterial surfaces is important to develop new biomaterials with improved properties. The phenomenon of peptide adsorption is determined by many parameters such environmental pH, surface topographical features, surface polarity, peptide structure, and/or surface and peptide electric charges. We assessed the effect of surface and peptide net charges on oligopeptide adsorption on synthetic surfaces under different conditions. We have also assessed the ability of immobilizing peptides on the surface generating covalent bonds or electrostatic attraction. Direct relation between the amount of peptide adsorbed on the surface and the difference in net charge between surface and peptides was determined. No relation between the difference in net charge and the ability to promote covalent bonds between peptide and surface was found. Competitive adsorption experiments confirmed these findings. Understanding the specific interactions during adsorption of peptides onto synthetic surfaces improves our ability to develop strategies for the efficient immobilization of oligopeptides on biomaterial surfaces.

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Relevant Properties for Immobilizing Short Peptides on Biosurfaces

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Bibliographical note

Keywords

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