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Frontiers of Materials Science

ISSN 2095-025X

ISSN 2095-0268(Online)

CN 11-5985/TB

Postal Subscription Code 80-974

2018 Impact Factor: 1.701

Front. Mater. Sci.    2015, Vol. 9 Issue (1) : 1-13    https://doi.org/10.1007/s11706-015-0274-z
REVIEW ARTICLE
Self-assembling peptide nanofiber hydrogels for central nervous system regeneration
Xi LIU1,2, Bin PI3, Hui WANG1, Xiu-Mei WANG2()
1. National Engineering Laboratory for Modern Silk, College of Textile and Clothing Engineering, Soochow University, Suzhou 215123, China
2. Institute for Regenerative Medicine and Biomimetic Materials, Key Laboratory of Advanced Materials, School of Materials Science and Engineering, Tsinghua University, Beijing 100084, China
3. Department of Orthopedics, The First Affiliated Hospital of Soochow University, Suzhou 215006, China
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Abstract

Central nervous system (CNS) presents a complex regeneration problem due to the inability of central neurons to regenerate correct axonal and dendritic connections. However, recent advances in developmental neurobiology, cell signaling, cell--matrix interaction, and biomaterials technologies have forced a reconsideration of CNS regeneration potentials from the viewpoint of tissue engineering and regenerative medicine. The applications of a novel tissue regeneration-inducing biomaterial and stem cells are thought to be critical for the mission. The use of peptide nanofiber hydrogels in cell therapy and tissue engineering offers promising perspectives for CNS regeneration. Self-assembling peptide undergo a rapid transformation from liquid to gel upon addition of counterions or pH adjustment, directly integrating with the host tissue. The peptide nanofiber hydrogels have mechanical properties that closely match the native central nervous extracellular matrix, which could enhance axonal growth. Such materials can provide an optimal three dimensional microenvironment for encapsulated cells. These materials can also be tailored with bioactive motifs to modulate the wound environment and enhance regeneration. This review intends to detail the recent status of self-assembling peptide nanofiber hydrogels for CNS regeneration.

Keywords self-assembling peptide      hydrogel      central nervous system (CNS)      nerve regeneration     
Corresponding Author(s): Xiu-Mei WANG   
About author:

Tongcan Cui and Yizhe Hou contributed equally to this work.

Online First Date: 17 December 2014    Issue Date: 02 March 2015
 Cite this article:   
Xi LIU,Bin PI,Hui WANG, et al. Self-assembling peptide nanofiber hydrogels for central nervous system regeneration[J]. Front. Mater. Sci., 2015, 9(1): 1-13.
 URL:  
https://academic.hep.com.cn/foms/EN/10.1007/s11706-015-0274-z
https://academic.hep.com.cn/foms/EN/Y2015/V9/I1/1
Fig.1  Molecular models of designer peptides and schematic illustrations of self-assembling peptide RADA16-I nanofiber scaffolds. RADA16-I contains 16 amino acids with alternating polar and nonpolar pattern and forms stable β-sheet double-tape structure. The side chains are distributed into two sides, polar side and non-polar side, to undergo self-assembly. Functional peptide motifs are extending out from the RADA16-I β-sheet double-tape. The typical atomic force microscopy (AFM) morphology of the self-assembling functionalized peptide solutions and scanning electron microscopy (SEM) morphology of the functionalized peptide nanofiber scaffold gel are also presented. (Reproduced from Ref. [101] with permission from the Royal Society of Chemistry)
Fig.2  Integration of implants within the injured spinal cord. (a) RADA implants integrated very well with host tissue, with no obvious cavities or gaps and only slight inflammation. Many host cells migrated into the implants, shown by 4′,6-diamidino-2-phenylindole hydrochloride (DAPI) staining. (b) Implantation of pre-cultured RADA with green fluorescent protein (GFP) NPCs, transplanted NPCs were found to migrate into the host tissue. (c) Alkaline phosphatase (AP) histochemistry staining showed (arrows) that blood vessels grew into the implants. (Reproduced with permission from Ref. [106], Copyright 2007 Elsevier)
Fig.3  Proposed model of MDPs nanofiber self-assembly. The nanofiber forms through the assembly of peptides stabilized by β-sheet hydrogen bonding down the long axis of the structure. This tape-like structure has a hydrophilic face and hydrophobic face. Two such tapes assemble to bury the hydrophobic interface and present hydrophilic and charged amino acids to the aqueous environment. Alteration hydrophobic amino acid and charged A amino acids result in different degree of self-assembly, morphology and mechanical properties. (Reproduced with permission from Ref. [130], Copyright 2007 American Chemical Society)
3D three dimensional
AFM atomic force microscopy
AP alkaline phosphatase
BBB Basso, Beattie and Bresnahan
BDNF brain-derived neurotrophic factor
CNS central nervous system
DAPI 4′,6-diamidino-2-phenylindole hydrochloride
ECM extracellular matrix
ELISA enzyme-linked immunosorbent assay
GFP green fluorescent protein
HE hematoxylin-eosin
MDP multidomain peptide
MEMRI manganese enhanced magnetic resonance imaging
NF neurofilament
NGF nerve growth factor
NPC neural progenitor cell
NSC neural stem cell
NT-3 neurotrophin 3
OEC olfactory ensheathing cell
PA peptide amphiphile
PBS phosphate buffered saline
PEG polyethylene glycol
PLA poly(lactic acid)
PLGA poly(lactic-co-glycolic acid)
SCI spinal cord injury
SEM scanning electron microscopy
SqRT-PCR semi-quantitative reverse transcription and polymerase chain reaction
TBI traumatic brain injury
VEGF vascular endothelial growth factor
  
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