Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2011 Sep 21;7(18):7927-7938.
doi: 10.1039/C1SM05329A.

Collagen Mimetic Peptides: Progress Towards Functional Applications

S Michael Yu  1 , Yang Li  2 , Daniel Kim  3
Affiliations

Collagen Mimetic Peptides: Progress Towards Functional Applications

S Michael Yu et al. Soft Matter. .

Abstract

Traditionally, collagen mimetic peptides (CMPs) have been used for elucidating the structure of the collagen triple helix and the factors responsible for its stabilization. The wealth of fundamental knowledge on collagen structure and cell-extracellular matrix (ECM) interactions accumulated over the past decades has led to a recent burst of research exploring the potential of CMPs to recreate the higher order assembly and biological function of natural collagens for biomedical applications. Although a large portion of such research is still at an early stage, the collagen triple helix has become a promising structural motif for engineering self-assembled, hierarchical constructs similar to natural tissue scaffolds which are expected to exhibit unique or enhanced biological activities. This paper reviews recent progress in the field of collagen mimetic peptides that bears both direct and indirect implications to engineering collagen-like materials for potential biomedical use. Various CMPs and collagen-like proteins that mimic either structural or functional characteristics of natural collagens are discussed with particular emphasis on providing helpful information to bioengineers and biomaterials scientists interested in collagen engineering.

PubMed Disclaimer

Figures

Fig. 1
Fig. 1
Triple helical structure and higher order assembly of collagen mimetic peptides. Collagen mimetic peptides have been designed to assemble into a long triple helical molecule by head-to-tail association (A, reproduced with permission from Ref. [21], © National Academy of Sciences), fibers by attractive interactions between CMP triple helices (B, reproduced with permission from Ref. [70] and , © Wiley and American Chemical Society, respectively), and micelle or vesicle-like structures by microphase separation of amphiphilic compounds (C, reproduced with permission from Ref. [79] and , © American Chemical Society).
Fig. 2
Fig. 2
Transmission electron micrographs of B. anthracis spores after negative staining (A and B, reproduced with permission from Ref. [43], © American Society for Microbiology), Scl1 protein after rotary shadowing (C, reproduced with permission from Ref. [44], © American Society for Biochemistry and Molecular Biology), and gold nanoparticles with self-assembled CMP monolayers (D). B. anthracis spores show densely packed collagen-like layers on their surfaces (double headed arrows): Strain 7702 which has 8 copies of (GPT)5GDTGTT sequence displays a thick layer (A), while strain 5725R with only 1 copy of the same sequence displays thin collagen like layer (B). Sc1 protein (streptococcal collagen like protein with charged amino acids) exhibits lollipop morphology similar to complement factors (C, block arrows). Self-assembled CMP layer provides colloidal stability to gold nanoparticles (D).
Fig. 3
Fig. 3
Fiber-like association of CMPs mediated by metal-ligand coordination. Fe2+ brings together three CMP triple helices by coordinating with Bpys incorporated into the CMP’s central amino acids: Structures of single strand CMP with central Bpy (A) and corresponding homotrimeric triple helix (B), and lateral CMP association by Fe2+ coordinating to three CMP triple helices (C). Reprinted with permission from Ref. [28], © American Chemical Society.
Fig. 4
Fig. 4
Schematic depiction of the hypothetical mechanism of CMP-collagen hybridization. Allowing melted CMP to fold in the presence of natural collagen triggers CMP hybridization with unstructured domains, either in the middle (shown in this figure) or end of the collagen molecules. Bottom right photo: transmission electron micrograph of reconstituted type I collagen fiber (mouse tail tendon) showing periodic localization of CMP conjugated gold nanoparticles (reproduced with permission from Ref. [33], © American Chemical Society).
Fig. 5
Fig. 5
Fluorescence confocal microscopy of a frozen, unfixed human liver carcinoma slice stained with carboxyfluorescene-CMP (in green) and CD31 antibody (in red).
Fig. 6
Fig. 6
The optical micrographs of human breast epithelial cells (3rd day culture) on collagen films treated with PEG-CMP (A, reproduced with permission from Ref. [34], © American Chemical Society), tube-like morphology of HUVEC cells in collagen gel treated with Glu8-CMP-8 and VEGF (B), and network morphology of group of HUVECs on collagen coating treated with QK-CMP (C).
Fig. 7
Fig. 7
Spatial gradients of CMP immobilized in 3D PEG-CMP hydrogel. CF-CMP that competes for triple helix was injected to the bottom right side of the gel. Particle tracking microrheology indicated gradual change in stiffness of the gel due to gradient of immobilized CMP that break-up the triple helical cross-links. Reproduced with permission from Ref. [37], © American Chemical Society.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Nimni ME. Collagen. CRC Press; Boca Raton: 1988.
    1. Shoulders MD, Raines RT. Annu. Rev. Biochem. 2009;78:929–958. - PMC - PubMed
    1. Birk DE, Bruckner P. In: Collagen. Brinckmann J, Notbohm H, Müller PK, editors. Vol. 247. Springer Berlin; Heidelberg, Berlin: 2005. pp. 185–205.
    1. Kassner A, Tiedemann K, Notbohm M, Ludwig T, Morgelin M, Reinhardt DP, Chu ML, Bruckner P, Grassel S. J. Mol. Biol. 2004;339:835–853. - PubMed
    1. Koch M, Foley JE, Hahn R, Zhou PH, Burgeson RE, Gerecke DR, Gordon MK. J. Biol. Chem. 2001;276:23120–23126. - PubMed