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

Overview

Journal Biores Open Access

Publisher Mary Ann Liebert

Specialty Biology

Date 2016 Dec 15

PMID 27965915

Citations 4

Authors

Kentaro Hozumi

Kyotaro Nakamura

Haruna Hori

Mari Miyagi

Rika Nagao

Keiko Takasaki

Fumihiko Katagiri

Yamato Kikkawa

Motoyoshi Nomizu

Affiliations

Soon will be listed here.

Abstract

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.

Citing Articles

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Estimation of a stronger heparin binding locus in fibronectin domain III using thermodynamics and molecular dynamics.

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Mixed Peptide-Conjugated Chitosan Matrices as Multi-Receptor Targeted Cell-Adhesive Scaffolds.

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