2000
DOI: 10.1073/pnas.97.12.6728
|View full text |Cite
|
Sign up to set email alerts
|

Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds

Abstract: A new type of self-assembling peptide (sapeptide) scaffolds that serve as substrates for neurite outgrowth and synapse formation is described. These peptide-based scaffolds are amenable to molecular design by using chemical or biotechnological syntheses. They can be tailored to a variety of applications. The sapeptide scaffolds are formed through the spontaneous assembly of ionic self-complementary ␤-sheet oligopeptides under physiological conditions, producing a hydrogel material. The scaffolds can support ne… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
2

Citation Types

10
823
1
4

Year Published

2002
2002
2017
2017

Publication Types

Select...
7
2

Relationship

0
9

Authors

Journals

citations
Cited by 1,082 publications
(844 citation statements)
references
References 39 publications
10
823
1
4
Order By: Relevance
“…7,8 These characteristics have attracted scientists to consider them as a class of designable bio-nanomaterials with new functions. 7,9−11 To date, amyloid fibers have been functionalized for applications in tissue engineering, 12,13 drug delivery, 14−16 enzyme immobilization, 17 metal nanowires, 18−20 protein films, 21 light-harvesting nanodevices, 8,22 retroviral gene transfer enhancer, 23 environmental carbon dioxide capture, 24 and enzyme-like catalysis. 25 Although first identified as pathological entities, amyloid fibers have evolved in living organisms from prokaryotes to eukaryotes to perform diverse functions, including signal transduction, 26 RNA granule formation, 27 memory persistence, 28 hormone storage, 29 and cell surface adhesion.…”
Section: ■ Introductionmentioning
confidence: 99%
“…7,8 These characteristics have attracted scientists to consider them as a class of designable bio-nanomaterials with new functions. 7,9−11 To date, amyloid fibers have been functionalized for applications in tissue engineering, 12,13 drug delivery, 14−16 enzyme immobilization, 17 metal nanowires, 18−20 protein films, 21 light-harvesting nanodevices, 8,22 retroviral gene transfer enhancer, 23 environmental carbon dioxide capture, 24 and enzyme-like catalysis. 25 Although first identified as pathological entities, amyloid fibers have evolved in living organisms from prokaryotes to eukaryotes to perform diverse functions, including signal transduction, 26 RNA granule formation, 27 memory persistence, 28 hormone storage, 29 and cell surface adhesion.…”
Section: ■ Introductionmentioning
confidence: 99%
“…Synthetic analogs of the natural ECMs were developed as 3-D scaffolds in an effort to accomplish in vivo-like environments in culture dishes, ex vivo tissue growth and engineering, and other scientific applications without posing health risks. One such material, PuraMatrix ™ , is a synthetic, self-assembling, peptide-based material that forms fibrous scaffolds and can be used for 3-D cell embedding or surface plating [19][20][21][22][23]. This nonanimal-derived material is non-immunogenic and can be used for in vivo studies.…”
Section: Introductionmentioning
confidence: 99%
“…14,18 A tunable peptide-based scaffold that has a fibrillar structure (could act as morphogenetic guide to cells) and is dynamically responsive to repeated strains caused either by cell motility, orientation or proliferation, might foster the growth of the developing tissue constructs. [19][20][21] The key to rapid recovery is a fast and reversible assembly-disassembly-reassembly process. Previous design of peptide based hydrogels rested on the principle of self-complementarity, i.e., spontaneous assembly of a single peptide chain complementary to itself.…”
Section: Introductionmentioning
confidence: 99%