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Biological activity of peptide-conjugated polyion complex matrices consisting of alginate and chitosan.
- Source :
-
Biopolymers [Biopolymers] 2017 Jan; Vol. 108 (1). - Publication Year :
- 2017
-
Abstract
- Peptide-conjugated polysaccharide matrices using bioactive laminin-derived peptides are useful biomaterials for tissue and cell engineering. Here, we demonstrate an easy handling preparation method for peptide-polysaccharide matrices using polyion complex with both alginate and chitosan. First, aldehyde-alginate was synthesized by oxidization of alginate using NaIO <subscript>4</subscript> , and then, reacted with Cys-peptides. Next, the peptide-alginate solution was added to a chitosan-coated plate, and the peptide-polyion complex matrices (peptide-PCMs) were prepared. The peptide-PCMs using an integrin αvβ3-binding peptide (A99a: ALRGDN, mouse laminin α1 chain 1145-1150) and an integrin α2β1-binding peptide (EF1XmR: RLQLQEGRLHFXFD, X = Nle, mouse laminin α1 chain 2751-2763) showed strong cell attachment activity in a dose-dependent manner. When we examined the effect of various spacers on the biological activity of A99a-PCM, hydrophobic and long spacers enhanced the cell attachment activity. Further, the A99a-PCM with the spacers strongly promoted neurite outgrowth. The polyion complex method is an easy way to obtain insolubilized matrix and is widely applicable for various polysaccharides. The peptide-PCM is useful as a biomaterial for cell and tissue engineering.<br /> (© 2016 Wiley Periodicals, Inc.)
- Subjects :
- Aldehydes chemistry
Amino Acid Sequence
Animals
Antibodies chemistry
Antibodies immunology
Cell Adhesion drug effects
Cell Line
Edetic Acid chemistry
Heparin chemistry
Humans
Integrin alpha1beta1 chemistry
Integrin alpha1beta1 immunology
Integrin alphaVbeta3 chemistry
Integrin alphaVbeta3 immunology
Laminin chemistry
Mice
Microscopy, Fluorescence
Neurites metabolism
Oxidation-Reduction
Peptides chemical synthesis
Peptides metabolism
Peptides pharmacology
Alginates chemistry
Chitosan chemistry
Peptides chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1097-0282
- Volume :
- 108
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biopolymers
- Publication Type :
- Academic Journal
- Accession number :
- 27603160
- Full Text :
- https://doi.org/10.1002/bip.22983