Biological activity of peptide-conjugated polyion complex matrices consisting of alginate and chitosan.
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 NaIO4, 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.
Department of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, 192-0392, Japan.
Chikara
C
Fujimori
Department of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, 192-0392, Japan.
Jun
J
Kumai
Department of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, 192-0392, Japan.
Kyotaro
K
Nakamura
Department of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, 192-0392, Japan.
Yingzi
Y
Gu
Department of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, 192-0392, Japan.
Fumihiko
F
Katagiri
Department of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, 192-0392, Japan.
Kentaro
K
Hozumi
Department of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, 192-0392, Japan.
Yamato
Y
Kikkawa
Department of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, 192-0392, Japan.
Motoyoshi
M
Nomizu
D000447:Aldehydes / Q000737:chemistry; D000464:Alginates / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000737:chemistry / Q000276:immunology; D002448:Cell Adhesion / Q000187:drug effects; D002460:Cell Line; D048271:Chitosan / Q000737:chemistry*; D004492:Edetic Acid / Q000737:chemistry; D006493:Heparin / Q000737:chemistry; D006801:Humans; D039222:Integrin alpha1beta1 / Q000737:chemistry / Q000276:immunology; D039302:Integrin alphaVbeta3 / Q000737:chemistry / Q000276:immunology; D007797:Laminin / Q000737:chemistry; D051379:Mice; D008856:Microscopy, Fluorescence; D016501:Neurites / Q000378:metabolism; D010084:Oxidation-Reduction; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology
D000447:Aldehydes; D000464:Alginates; D000906:Antibodies; D039222:Integrin alpha1beta1; D039302:Integrin alphaVbeta3; D007797:Laminin; D010455:Peptides; C084098:laminin A; D006493:Heparin; D048271:Chitosan; D004492:Edetic Acid
alginate; chitosan; integrin; laminin; polyion complex