A CMP-based method for tunable, cell-mediated gene delivery from collagen scaffolds

2014 ◽  
Vol 2 (46) ◽  
pp. 8174-8185 ◽  
Author(s):  
M. A. Urello ◽  
K. L. Kiick ◽  
M. O. Sullivan
Keyword(s):  
Gene Delivery ◽  
Collagen Scaffolds ◽  
Mimetic Peptides ◽  
Collagen Mimetic Peptides

Collagen mimetic peptides (CMP)s were used to tailor release vs. retention of DNA polyplexes from collagen while preserving polyplex activity.

Immobilization of Growth Factors on Collagen Scaffolds Mediated by Polyanionic Collagen Mimetic Peptides and Its Effect on Endothelial Cell Morphogenesis

2008 ◽  
Vol 9 (10) ◽  
pp. 2929-2936 ◽  
Author(s):  
Allen Y. Wang ◽  
Shirley Leong ◽  
Yu-Chuan Liang ◽  
Ru Chih C. Huang ◽  
Christopher S. Chen ◽  
...  
Keyword(s):  
Growth Factors ◽  
Endothelial Cell ◽  
Cell Morphogenesis ◽  
Collagen Scaffolds ◽  
Mimetic Peptides ◽  
Collagen Mimetic Peptides

scholarly journals Supramolecular Nanofibers from Collagen-Mimetic Peptides Bearing Various Aromatic Groups at N-Termini via Hierarchical Self-Assembly

2021 ◽  
Vol 22 (9) ◽  
pp. 4533
Author(s):  
Tomoyuki Koga ◽  
Shinya Kingetsu ◽  
Nobuyuki Higashi
Keyword(s):  
Self Assembly ◽  
Triple Helix ◽  
Wavelength Conversion ◽  
Nile Red ◽  
Tem Analysis ◽  
Mimetic Peptides ◽  
Collagen Mimetic Peptides ◽  
Potential Applications ◽  
Hydrophobic Molecule ◽  
Emission Behavior

Self-assembly of artificial peptides has been widely studied for constructing nanostructured materials, with numerous potential applications in the nanobiotechnology field. Herein, we report the synthesis and hierarchical self-assembly of collagen-mimetic peptides (CMPs) bearing various aromatic groups at the N-termini, including 2-naphthyl, 1-naphtyl, anthracenyl, and pyrenyl groups, into nanofibers. The CMPs (R-(GPO)n: n > 4) formed a triple helix structure in water at 4 °C, as confirmed via CD analyses, and their conformations were more stable with increasing hydrophobicity of the terminal aromatic group and peptide chain length. The resulting pre-organized triple helical CMPs showed diverse self-assembly into highly ordered nanofibers, reflecting their slight differences in hydrophobic/hydrophilic balance and configuration of aromatic templates. TEM analysis demonstrated that 2Np-CMPn (n = 6 and 7) and Py-CMP6 provided well-developed natural collagen-like nanofibers and An-CMPn (n = 5–7) self-assembled into rod-like micelle fibers. On the other hand, 2Np-CMP5 and 1Np-CMP6 were unable to form nanofibers under the same conditions. Furthermore, the Py-CMP6 nanofiber was found to encapsulate a guest hydrophobic molecule, Nile red, and exhibited unique emission behavior based on the specific nanostructure. In addition to the ability of CMPs to bind small molecules, their controlled self-assembly enables their versatile utilization in drug delivery and wavelength-conversion nanomaterials.

scholarly journals Effects of Surface-Bound Collagen-Mimetic Peptides on Macrophage Uptake and Immunomodulation

2020 ◽  
Vol 8 ◽  
Author(s):  
Andrew T. Rowley ◽  
Vijaykumar S. Meli ◽  
Natalie J. Wu-Woods ◽  
Esther Y. Chen ◽  
Wendy F. Liu ◽  
...  
Keyword(s):  
Mimetic Peptides ◽  
Collagen Mimetic Peptides ◽  
Macrophage Uptake

scholarly journals Collagen mimetic peptide discs promote assembly of a broad range of natural protein fibers through hydrophobic interactions

2017 ◽  
Vol 15 (28) ◽  
pp. 5893-5898 ◽  
Author(s):  
Kenneth McGuinness ◽  
Vikas Nanda
Keyword(s):  
Hydrophobic Interactions ◽  
Mimetic Peptide ◽  
Natural Protein ◽  
Protein Fibers ◽  
Mimetic Peptides ◽  
Collagen Mimetic Peptides

Collagen mimetic peptides bind to a variety of fiber-forming proteins through complementary hydrophobic interactions, resulting in discs-on-a-string nanostructures and bundling of fibers.

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