scholarly journals Toward Activatable Collagen Mimics: Combining DEPSI “Switch” Defects and Template‐Guided Self‐Organization to Control Collagen Mimetic Peptides

2021 ◽  
pp. 2100070
Author(s):  
Matthias Röber ◽  
Thomas Scheibel ◽  
Hans G. Börner
Keyword(s):  
Self Organization ◽  
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.

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.

Synthesis and incorporation of an advanced lipid peroxidation end-product building block into collagen mimetic peptides

2017 ◽  
Vol 53 (60) ◽  
pp. 8459-8462 ◽  
Author(s):  
Iman Kavianinia ◽  
Sung-Hyun Yang ◽  
Harveen Kaur ◽  
Paul W. R. Harris ◽  
Renwick C. J. Dobson ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Building Block ◽  
End Products ◽  
Mimetic Peptides ◽  
Collagen Mimetic Peptides ◽  
And Oxidative Stress

Advanced lipid peroxidation end-products (ALEs) accumulate with ageing and oxidative stress-related diseases.

scholarly journals Template-tethered collagen mimetic peptides for studying heterotrimeric triple-helical interactions

Biopolymers ◽  
2010 ◽  
Vol 95 (2) ◽  
pp. 94-104 ◽  
Author(s):  
Yang Li ◽  
Xiao Mo ◽  
Daniel Kim ◽  
S. Michael Yu
Keyword(s):  
Mimetic Peptides ◽  
Collagen Mimetic Peptides

scholarly journals Sequence-specific response of collagen-mimetic peptides to osmotic pressure

MRS Bulletin ◽  
2021 ◽  
Author(s):  
Lorena Ruiz-Rodriguez ◽  
Philip Loche ◽  
Lise Thornfeldt Hansen ◽  
Roland R. Netz ◽  
Peter Fratzl ◽  
...  
Keyword(s):  
Osmotic Pressure ◽  
Triple Helix ◽  
Materials Science ◽  
Mechanical Function ◽  
Fibre Direction ◽  
Mimetic Peptides ◽  
Native Collagen ◽  
Collagen Mimetic Peptides ◽  
Collagen Molecules ◽  
Tissue Tension

Abstract Native collagen molecules usually contract upon dehydration, but the details of their interaction with water are poorly understood. Previous molecular modeling studies indicated a spatially inhomogeneous response, with a combination of local axial expansion and contraction. Such sequence-dependent effects are difficult to study with native collagen. In this article, we use collagen-mimetic peptides (CMPs) to investigate the effect of osmotic pressure on several collagen-mimetic sequences. Synchrotron x-ray diffraction combined with molecular dynamics simulations shows that CMPs pack differently depending on osmotic pressure and exhibit changes in the helical rise per residue of individual molecules. Infrared spectroscopy reveals that osmotic pressure affects the stability of the triple helix through changes in triple helix-stabilizing hydrogen bonds. Surprisingly, CMPs with the canonical collagen sequence glycine–proline–hydroxyproline are found to elongate upon dehydration, while sequence modifications are able to reverse this tendency. This strongly suggests that the overall contraction of native collagen molecules is not programmed into the canonical sequence but is specific to local amino acids that substitute for proline or hydroxyproline along the protein chain. Collagen is an essential protein in mammalian extracellular tissues and a better understanding of its mechanical function is important both from a materials science and from a biomedical viewpoint. Recently, collagen has been shown to contract along the fibre direction when subjected to osmotic stress, a process that could play important roles in strengthening bone and in developing tissue tension during extracellular matrix development. The present work uses collagen-like short peptides to show that the canonical collagen sequence is not responsible for this contraction. The conclusion is that the collagen amino acid sequence must have evolved to include guest sequences within the canonical glycine-proline-hydroxyproline repeat that provide the observed contractility. Impact statement Collagen is an essential protein in mammalian extracellular tissues and a better understanding of its mechanical function is important both from a materials science and from a biomedical viewpoint. Recently, collagen has been shown to contract along the fibre direction when subjected to osmotic stress, a process that could play important roles in strengthening bone and in developing tissue tension during extracellular matrix development. The present work uses collagen-like short peptides to show that the canonical collagen sequence is not responsible for this contraction. The conclusion is that the collagen amino acid sequence must have evolved to include guest sequences within the canonical glycine-proline-hydroxyproline that provide the observed contractility. Graphic Abstract

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