Highly porous protein‐based 3D scaffolds with different collagen concentrates for potential application in tissue engineering

ABSTRACT Different researchers have developed protein‐based scaffolds for tissue engineering, although few of them have combined their development with previous characterization of the raw material used. The main objective of this work was to characterize four Type I collagen protein concentrates fr...

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Bibliographic Details
Published in:Journal of applied polymer science 2019-10, Vol.136 (37), p.n/a
Main Authors: Perez‐Puyana, V. M., Jiménez‐Rosado, M., Romero, A., Guerrero, A.
Format: Article
Language:English
Subjects:
Chemical composition
Collagen
Deformation
Fish
Formability
Glycine
Materials science
Organic chemistry
Polymers
Pork
Porosity
Proteins
Scaffolds
Tissue engineering
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Summary:ABSTRACT Different researchers have developed protein‐based scaffolds for tissue engineering, although few of them have combined their development with previous characterization of the raw material used. The main objective of this work was to characterize four Type I collagen protein concentrates from different sources (pork HI95, pork T95, turkey, and fish) and study their use as scaffolds for tissue engineering. Thus, the chemical and amino acid composition, protein solubility, and Z‐potential of the different concentrates were analyzed in the pH range between 2 and 12. In addition, the mechanical and structural properties of the different scaffolds were compared. The initial characterization of the four concentrates shows similarities, such as a typical amino acid profile and an isoelectric point between pH 5 and 6. In fact, differences based on composition, namely, systems with higher protein concentration, results in more deformable scaffolds, whereas the ones processed from fish collagen, with a higher glycine percentage, shows the highest porosity and pore sizes. © 2019 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2019, 136, 47954. Schematic overview of the scaffold and its structural and mechanical properties.
ISSN:0021-8995
1097-4628
DOI:10.1002/app.47954