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Bioengineered Collagens

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Fibrous Proteins: Structures and Mechanisms

Part of the book series: Subcellular Biochemistry ((SCBI,volume 82))

Abstract

There is a great deal of interest in obtaining recombinant collagen as an alternative source of material for biomedical applications and as an approach for obtaining basic structural and biological information. However, application of recombinant technology to collagen presents challenges, most notably the need for post-translational hydroxylation of prolines for triple-helix stability. Full length recombinant human collagens have been successfully expressed in cell lines, yeast, and several plant systems, while collagen fragments have been expressed in E. coli. In addition, bacterial collagen-like proteins can be expressed in high yields in E. coli and easily manipulated to incorporate biologically active sequences from human collagens. These expression systems allow manipulation of biologically active sequences within collagen, which has furthered our understanding of the relationships between collagen sequences, structure and function. Here, recombinant studies on collagen interactions with cell receptors, extracellular matrix proteins, and matrix metalloproteinases are reviewed, and discussed in terms of their potential biomaterial and biomedical applications.

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Abbreviations

CL:

collagen domain of the bacterial protein Scl2

D:

67 nm axial periodicity

DDR:

discoidin domain receptor

ECM:

extracellular matrix

EGF:

epidermal growth factor

Fn:

fibronectin

IL-2:

interleukin-2

MMP:

matrix metalloproteinase

P4H:

prolyl 4-hydroxylase

Scl2:

Streptococcus pyogenes collagen-like protein 2

Tm:

melting temperature

V:

trimerization domain of Scl2

vWF:

von Willebrand factor

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Acknowledgment

This work was supported in part through NIH grants EB011620 and GM60048 (BB).

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Authors and Affiliations

  1. Department of Biomedical Engineering, Tufts University, Medford, MA, USA

    Barbara Brodsky

  2. CSIRO Manufacturing, Bayview Avenue, Clayton, VIC, 3169, Australia

    John A. M. Ramshaw

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  1. Barbara Brodsky
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  2. John A. M. Ramshaw
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Correspondence to Barbara Brodsky .

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Editors and Affiliations

  1. Institute of Fundamental Sciences and Riddet Institute, Massey University, Palmerston North, New Zealand

    David A.D. Parry

  2. Muscle Contraction Group, School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, United Kingdom

    John M. Squire

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Brodsky, B., Ramshaw, J.A.M. (2017). Bioengineered Collagens. In: Parry, D., Squire, J. (eds) Fibrous Proteins: Structures and Mechanisms. Subcellular Biochemistry, vol 82. Springer, Cham. https://doi.org/10.1007/978-3-319-49674-0_18

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