Self-assembled Biodegradable Nanoparticles and Polysaccharides as Biomimetic ECM Nanostructures for the Synergistic effect of RGD and BMP-2 on Bone Formation

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Abstract

Producing biomimetic extracellular matrix (ECM) is an effective approach to improve biocompatibility of medical devices. In this study, biomimetic ECM nanostructures are constructed through layer-by-layer self-assembling positively charged chitosan (Chi), negatively charged oxidized sodium alginate (OAlg), and positively charged bovine serum albumin (BSA)-based nanoparticles. The BSA-based nanoparticles in the self-assembled films not only result in porous nanostructures similar to natural ECM, but also preserve the activity and realize the sustained release of Bone morphogenetic protein-2 (BMP-2). The results of bone marrow stem cells (BMSCs) culture demonstrate that the penta-peptide glycine-arginine-glycine-aspartate-serine (GRGDS) grafted Chi/OAlg films favor cell adhesion and proliferation. GRGDS and BMP-2 in biomimetic ECM nanostructures synergistically promote BMSC functions and new bone formation. The RGD and BMP incorporated biomimetic ECM coatings could be applied on a variety of biomedical devices to improve the bioactivity and biocompatibility.

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Most cited references 28

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Advantages of RGD peptides for directing cell association with biomaterials.

Susan Bellis (2011)

Despite many years of in vitro research confirming the effectiveness of RGD in promoting cell attachment to a wide variety of biomaterials, animal studies evaluating tissue responses to implanted RGD-functionalized substrates have yielded more variable results. The goals of this report are to present some of the reasons why cell culture studies may not always reliably predict in vivo responses, and more importantly, to highlight potential applications that may benefit from the use of RGD peptides. Copyright © 2011 Elsevier Ltd. All rights reserved.

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Integrin structure, allostery, and bidirectional signaling.

B Mahalingam, J Xiong, M. Arnaout (2004)

Alphabeta heterodimeric integrins mediate dynamic adhesive cell-cell and cell-extracellular matrix (ECM) interactions in metazoa that are critical in growth and development, hemostasis, and host defense. A central feature of these receptors is their capacity to change rapidly and reversibly their adhesive functions by modulating their ligand-binding affinity. This is normally achieved through interactions of the short cytoplasmic integrin tails with intracellular proteins, which trigger restructuring of the ligand-binding site through long-range conformational changes in the ectodomain. Ligand binding in turn elicits conformational changes that are transmitted back to the cell to regulate diverse responses. The publication of the integrin alphaVbeta3 crystal structure has provided the context for interpreting decades-old biochemical studies. Newer NMR, crystallographic, and EM data, reviewed here, are providing a better picture of the dynamic integrin structure and the allosteric changes that guide its diverse functions.

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Integrin activation and internalization on soft ECM as a mechanism of induction of stem cell differentiation by ECM elasticity.

Xiaofei Chen, W.-G. Zhang, Shu Chien … (2011)

The mechanism by which ECM elasticity induces lineage specification of stem cells has not been clearly understood. Integrins are well-documented mechanosensors that are positioned at the beginning of the sensing pathway. By using an antibody specifically recognizing the active conformation of β1 integrin, we observed that β1 integrin activation in bone marrow mesenchymal stem cells (BMMSCs) was induced by soft substrate to a significantly greater degree than by stiff substrate. In contrast, however, the level of cell surface integrin on soft substrate was significantly lower than that on stiff substrate. Soft substrate markedly enhanced the internalization of integrin, and this internalization was mediated mainly through caveolae/raft-dependent endocytosis. The inhibition of integrin internalization blocked the neural lineage specification of BMMSCs on soft substrate. Furthermore, soft substrate also repressed the bone morphogenetic protein (BMP)/Smad pathway at least partially through integrin-regulated BMP receptor endocytosis. A theoretical analysis based on atomic force microscopy (AFM) data indicated that integrin-ligand complexes are more easily ruptured on soft substrate; this outcome may contribute to the enhancement of integrin internalization on soft substrate. Taken together, our results suggest that ECM elasticity affects integrin activity and trafficking to modulate integrin BMP receptor internalization, thus contributing to stem cell lineage specification.

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Author and article information

Journal

Journal ID (nlm-ta): Sci Rep

Journal ID (iso-abbrev): Sci Rep

Title: Scientific Reports

Publisher: Nature Publishing Group

ISSN (Electronic): 2045-2322

Publication date (Electronic): 28 April 2016

Publication date Collection: 2016

Volume: 6

Electronic Location Identifier: 25090

Affiliations

[1 ]Key Lab of Advanced Technologies of Materials, Ministry of Education, School of Materials Science and Engineering, Southwest Jiaotong University , Chengdu, Sichuan, 610031, China

[2 ]National Engineering Research Center for Biomaterials, Genome Research Center for Biomaterials, Sichuan University , Chengdu, Sichuan, 610064, China

[3 ]School of Materials Science and Engineering, South China University of Technology , Guangzhou 510641, China

[4 ]School of Chinese Medicine, Faculty of Medicine, The Chinese University of Hong Kong , Shatin, Hong Kong, China

[5 ]Laboratory of Stem Cell and Tissue Engineering, State Key Laboratory of Biotherapy, Sichuan University , Chengdu, 610041, China

Author notes

[a ] luxiong_2004@ 123456163.com

[*]

These authors contributed equally to this work.

Article

Publisher Item ID: srep25090

DOI: 10.1038/srep25090

PMC ID: 4848559

PubMed ID: 27121121

SO-VID: 08548e52-5f69-4010-93ef-263a4e61841d

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Self-assembled Biodegradable Nanoparticles and Polysaccharides as Biomimetic ECM Nanostructures for the Synergistic effect of RGD and BMP-2 on Bone Formation

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Most cited references 28

Advantages of RGD peptides for directing cell association with biomaterials.

Integrin structure, allostery, and bidirectional signaling.

Integrin activation and internalization on soft ECM as a mechanism of induction of stem cell differentiation by ECM elasticity.

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