Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan

Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan

Mimicking the biological function of the extracellular matrix is an approach to developing cell adhesive biomaterials. The RGD peptide, derived from fibronectin (Fn), mainly binds to integrin αvβ3 and has been widely used as a cell adhesive peptide on various biomaterials. However, cell adhesion to...

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Main Authors: Hozumi, Kentaro, Nakamura, Kyotaro, Hori, Haruna, Miyagi, Mari, Nagao, Rika, Takasaki, Keiko, Katagiri, Fumihiko, Kikkawa, Yamato, Nomizu, Motoyoshi
Format: Online
Language:English
Published: Mary Ann Liebert, Inc. 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5144869/
id pubmed-5144869
recordtype oai_dc
spelling pubmed-51448692016-12-13 Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan Hozumi, Kentaro Nakamura, Kyotaro Hori, Haruna Miyagi, Mari Nagao, Rika Takasaki, Keiko Katagiri, Fumihiko Kikkawa, Yamato Nomizu, Motoyoshi Original Research Article Mimicking the biological function of the extracellular matrix is an approach to developing cell adhesive biomaterials. The RGD peptide, derived from fibronectin (Fn), mainly binds to integrin αvβ3 and has been widely used as a cell adhesive peptide on various biomaterials. However, cell adhesion to Fn is thought to be mediated by several integrin subtypes and syndecans. In this study, we synthesized an RGD-containing peptide (FIB1) and four integrin α4β1-binding-related motif-containing peptides (LDV, IDAPS, KLDAPT, and PRARI) and constructed peptide-chitosan matrices. The FIB1-chitosan matrix promoted human dermal fibroblast (HDF) attachment, and the C-terminal elongated PRARI (ePRARI-C)-conjugated chitosan matrix significantly promoted HDF attachment through integrin α4β1 and syndecan binding. Next, we constructed a mixed ePRARI-C- and FIB1-chitosan matrix to develop a Fn mimetic biomaterial. The mixed ePRARI-C/FIB1-chitosan matrix promoted significantly better cell attachment and neurite outgrowth compared to those of either ePRARI-C- or FIB1-chitosan matrices. HDF adhesion to the ePRARI-C/FIB1-chitosan matrix was mediated by integrin, α4β1, α5β1, and αvβ3, similar to HDF adhesion to Fn. These data suggest that an ePRARI-C/FIB1-chitosan matrix can be used as a tool to analyze the multiple functions of Fn and can serve as a Fn-mimetic biomaterial. Mary Ann Liebert, Inc. 2016-11-01 /pmc/articles/PMC5144869/ /pubmed/27965915 http://dx.doi.org/10.1089/biores.2016.0037 Text en © Kentaro Hozumi et al. 2016; Published by Mary Ann Liebert, Inc. This Open Access article is distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Hozumi, Kentaro
Nakamura, Kyotaro
Hori, Haruna
Miyagi, Mari
Nagao, Rika
Takasaki, Keiko
Katagiri, Fumihiko
Kikkawa, Yamato
Nomizu, Motoyoshi
spellingShingle Hozumi, Kentaro
Nakamura, Kyotaro
Hori, Haruna
Miyagi, Mari
Nagao, Rika
Takasaki, Keiko
Katagiri, Fumihiko
Kikkawa, Yamato
Nomizu, Motoyoshi
Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan
author_facet Hozumi, Kentaro
Nakamura, Kyotaro
Hori, Haruna
Miyagi, Mari
Nagao, Rika
Takasaki, Keiko
Katagiri, Fumihiko
Kikkawa, Yamato
Nomizu, Motoyoshi
author_sort Hozumi, Kentaro
title Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan
title_short Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan
title_full Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan
title_fullStr Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan
title_full_unstemmed Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan
title_sort mixed fibronectin-derived peptides conjugated to a chitosan matrix effectively promotes biological activities through integrins, α4β1, α5β1, αvβ3, and syndecan
description Mimicking the biological function of the extracellular matrix is an approach to developing cell adhesive biomaterials. The RGD peptide, derived from fibronectin (Fn), mainly binds to integrin αvβ3 and has been widely used as a cell adhesive peptide on various biomaterials. However, cell adhesion to Fn is thought to be mediated by several integrin subtypes and syndecans. In this study, we synthesized an RGD-containing peptide (FIB1) and four integrin α4β1-binding-related motif-containing peptides (LDV, IDAPS, KLDAPT, and PRARI) and constructed peptide-chitosan matrices. The FIB1-chitosan matrix promoted human dermal fibroblast (HDF) attachment, and the C-terminal elongated PRARI (ePRARI-C)-conjugated chitosan matrix significantly promoted HDF attachment through integrin α4β1 and syndecan binding. Next, we constructed a mixed ePRARI-C- and FIB1-chitosan matrix to develop a Fn mimetic biomaterial. The mixed ePRARI-C/FIB1-chitosan matrix promoted significantly better cell attachment and neurite outgrowth compared to those of either ePRARI-C- or FIB1-chitosan matrices. HDF adhesion to the ePRARI-C/FIB1-chitosan matrix was mediated by integrin, α4β1, α5β1, and αvβ3, similar to HDF adhesion to Fn. These data suggest that an ePRARI-C/FIB1-chitosan matrix can be used as a tool to analyze the multiple functions of Fn and can serve as a Fn-mimetic biomaterial.
publisher Mary Ann Liebert, Inc.
publishDate 2016
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5144869/
_version_ 1613766234004783104

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