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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Fan, Wei
Aalborg University
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (9/9 displayed)
- 2018Recent Advances on OTA Testing for 5G Antenna Systems in Multi-probe Anechoic Chamber Setupscitations
- 2018Over-the-air Radiated Testing of Millimeter-Wave Beam-steerable Devices in a Cost-Effective Measurement Setupcitations
- 2016Wideband MIMO Channel Capacity Analysis in Multiprobe Anechoic Chamber Setupscitations
- 2016Emulating Ray-Tracing Channels in Multi-probe Anechoic Chamber Setups for Virtual Drive Testingcitations
- 2015Over the air test
- 2013COST IC1004 Temporary Document: Characterization of Interference for Over the Air Terminal Testing
- 2012A biphasic scaffold design combined with cell sheet technology for simultaneous regeneration of alveolar bone/periodontal ligament complexcitations
- 2011Bioactive SrO-SiO<sub>2</sub> glass with well-ordered mesopores: Characterization, physiochemistry and biological propertiescitations
- 2010Self-assembly of fibronectin mimetic peptide-amphiphile nanofiberscitations
Places of action
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article
Self-assembly of fibronectin mimetic peptide-amphiphile nanofibers
Abstract
<p>Single-tailed peptide-amphiphiles have been shown to form nanofibers in solution and gel after screening of their electrostatic charges, and those containing cell-binding motifs are promising as tissue engineering scaffolds. A fibronectin-mimetic peptide sequence was developed, containing both the primary binding domain RGD and the synergy binding domain PHSRN, which has shown superior cell adhesion properties over simple RGD sequences and fibronectin in 2D culture. In order to test this sequence in a 3D environment in the future, we have designed a C<sub>16</sub> single-tailed peptide-amphiphile, PR-g (with a peptide headgroup of GGGSSPHSRN(SG)<sub>5</sub>RGDSP), that forms nanofibers and a gel in solution without any screening of its positive charge. In this study, we characterized the self-assembly properties of the PR-g peptide-amphiphile via critical micelle concentration (CMC) measurements, circular dichroism (CD) spectroscopy, cryo-transmission electron microscopy (cryo-TEM), small angle neutron scattering (SANS), and rheology measurements. The CMC of the PR-g amphiphile was determined to be 38 μM. CD measurements showed that even though the peptide formed an unordered secondary structure, the peptide-amphiphile's spectrum after aging resembled more the spectrum, of an α+β protein. Cryo-TEM images of a 100 μM peptide-amphiphile solution showed individual nanofibers with a diameter of approximately 10 nm and lengths on the order of several micrometers. Images taken at higher concentrations (1 mM) show a high degree of bundling among the nanofibers, and at even higher concentrations (3 and 4 mM) SANS measurements also indicated that the peptide-amphiphile formed rod-shaped structures in solution. The peptide-amphiphile gel was monitored, by parallel-plate rheometry, and the elastic modulus (G′) was greater than the viscous modulus (G″), which indicates that PR-g forms a gel. The shear modulus for a 2 day old gel was measured to be approximately 500 Pa, which is within the modulus range for living tissue; thus, the PR-g gel shows potential as a possible scaffold for tissue engineering.</p>