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.

scholarly journals Conducting polymer nanoparticles decorated with collagen mimetic peptides for collagen targeting

2014 ◽  
Vol 50 (95) ◽  
pp. 15045-15048 ◽  
Author(s):  
José Luis Santos ◽  
Yang Li ◽  
Heidi R. Culver ◽  
Michael S. Yu ◽  
Margarita Herrera-Alonso
Keyword(s):  
Conducting Polymer ◽  
Polymer Nanoparticles ◽  
Mimetic Peptide ◽  
Mimetic Peptides ◽  
Collagen Mimetic Peptides

We report on the formation of conducting polymer nanoparticles (CPNs), stabilized by a collagen mimetic peptide (CMP)-polymer amphiphile.

scholarly journals Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions

2008 ◽  
Vol 105 (25) ◽  
pp. 8513-8518 ◽  
Author(s):  
M. A. Cejas ◽  
W. A. Kinney ◽  
C. Chen ◽  
J. G. Vinter ◽  
H. R. Almond ◽  
...  
Keyword(s):  
Self Assembly ◽  
Triple Helix ◽  
Hydrophobic Interactions ◽  
Mimetic Peptides ◽  
Collagen Mimetic Peptides

scholarly journals Optimization of interstrand interactions enables burn detection with a collagen-mimetic peptide

2019 ◽  
Vol 17 (46) ◽  
pp. 9906-9912 ◽  
Author(s):  
Jesús M. Dones ◽  
I. Caglar Tanrikulu ◽  
Jenu V. Chacko ◽  
Alexandra B. Schroeder ◽  
Trish T. Hoang ◽  
...  
Keyword(s):  
Ex Vivo ◽  
Mimetic Peptide ◽  
Mimetic Peptides ◽  
Collagen Mimetic Peptides

The modulation of interstrand steric clashes can shift the preference of collagen-mimetic peptides from homotrimer to heterotrimer formation, enabling the detection of burn-damaged tissue ex vivo.

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 Establishment of Collagen: Hydroxyapatite/BMP-2 Mimetic Peptide Composites

Materials ◽  
2020 ◽  
Vol 13 (5) ◽  
pp. 1203
Author(s):  
Liane Schuster ◽  
Nina Ardjomandi ◽  
Marita Munz ◽  
Felix Umrath ◽  
Christian Klein ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Cost Effective ◽  
Quartz Crystals ◽  
Mimetic Peptide ◽  
Glutamic Acid Residue ◽  
Hydroxyapatite Composite ◽  
Mimetic Peptides ◽  
Periosteal Cells

Extensive efforts were undertaken to develop suitable biomaterials for tissue engineering (TE) applications. To facilitate clinical approval processes and ensure the success of TE applications, bioinspired concepts are currently focused on. Working on bone tissue engineering, we describe in the present study a method for biofunctionalization of collagen/hydroxyapatite composites with BMP-2 mimetic peptides. This approach is expected to be fundamentally transferable to other tissue engineering fields. A modified BMP-2 mimetic peptide containing a negatively charged poly-glutamic acid residue (E7 BMP-2 peptide) was used to bind positively charged hydroxyapatite (HA) particles by electrostatic attraction. Binding efficiency was biochemically detected to be on average 85% compared to 30% of BMP-2 peptide without E7 residue. By quartz crystal microbalance (QCM) analysis, we could demonstrate the time-dependent dissociation of the BMP-2 mimetic peptides and the stable binding of the E7 BMP-2 peptides on HA-coated quartz crystals. As shown by immunofluorescence staining, alkaline phosphatase expression is similar to that detected in jaw periosteal cells (JPCs) stimulated with the whole BMP-2 protein. Mineralization potential of JPCs in the presence of BMP-2 mimetic peptides was also shown to be at least similar or significantly higher when low peptide concentrations were used, as compared to JPCs cultured in the presence of recombinant BMP-2 controls. In the following, collagen/hydroxyapatite composite materials were prepared. By proliferation analysis, we detected a decrease in cell viability with increasing HA ratios. Therefore, we chose a collagen/hydroxyapatite ratio of 1:2, similar to the natural composition of bone. The following inclusion of E7 BMP-2 peptides within the composite material resulted in significantly elevated long-term JPC proliferation under osteogenic conditions. We conclude that our advanced approach for fast and cost-effective scaffold preparation and biofunctionalization is suitable for improved and prolonged JPC proliferation. Further studies should prove the functionality of composite scaffolds in vivo.

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.

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