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Functionalized self-assembling peptide nanofiber hydrogel as a scaffold for rabbit nucleus pulposus cells

✍ Scribed by Baichuan Wang; Yongchao Wu; Zengwu Shao; Shuhua Yang; Biao Che; Caixia Sun; Zhilin Ma; Yannan Zhang


Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
516 KB
Volume
100A
Category
Article
ISSN
1549-3296

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✦ Synopsis


Abstract

In this study, a new functionalized peptide RLN was designed containing the bioactive motif link N, the amino terminal peptide of link protein. A link N nanofiber scaffold (LN‐NS) was self‐assembled by mixing peptide solution of RLN and RADA16. The characterization of LN‐NS was tested using atomic force microscopy (AFM). The biocompatibility and bioactivity of this nanofiber scaffold for rabbit nucleus pulposus cells (NPCs) were also evaluated. This designer functionalized nanofiber scaffold exhibited little cytotoxicity and promoted NPCs adhesion obviously. In three‐dimensional cell culture experiments, confocal reconstructed images testified that the functionalized LN‐NS‐guided NPCs migration from the surface into the hydrogel considerably, in which the RADA16 scaffold did not. Moreover, the functionalized LN‐NS significantly stimulated the biosynthesis of extracelluar matrices (ECM) by NPCs. Our findings demonstrate that the functionalized nanofiber scaffold containing link N had excellent biocompatibility and bioactivity with rabbit NPCs and could be useful in the nucleus pulposus regeneration. © 2011 Wiley Periodicals, Inc. J Biomed Mater Res Part A, 2012.


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The effect of a self-assembling peptide
✍ Hui Meng; Liyan Chen; Zhaoyang Ye; Songtao Wang; Xiaojun Zhao 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 998 KB

## Abstract RADARADARADARADA (RADA16‐I) peptide, consisting of 16 alternating hydrophobic and hydrophilic (also alternating negative and positive charges) amino acids, forms extremely stable β‐pleated sheet structure and then self‐assembles into nanofibers to produce high‐order interwoven nanofiber