Difference between revisions of "Part:BBa K3833000"
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Scl2 is easily expressed in E. coli and lacks the requirement for post-translational modifications; this makes it a useful alternative to recombinant human collagen expressed in eukaryotic organisms[1]. For these reasons, we chose Scl2 as the backbone for Collatrix — a collagen-mimetic gradient hydrogel for bone-soft tissue interfaces. | Scl2 is easily expressed in E. coli and lacks the requirement for post-translational modifications; this makes it a useful alternative to recombinant human collagen expressed in eukaryotic organisms[1]. For these reasons, we chose Scl2 as the backbone for Collatrix — a collagen-mimetic gradient hydrogel for bone-soft tissue interfaces. | ||
− | Scl2 can be modified to specific locations with common mammalian cell binding sites, such as fibronectin and integrin [2]. After is it produced, it can be cross-linked both chemically (with the use of glutaraldehyde) and with UV light in order to create hydrogels to serve as scaffolds for cell growth. | + | Scl2 can be modified to specific locations with common mammalian cell binding sites, such as fibronectin and integrin [2]. After is it produced, it can be cross-linked both chemically (with the use of glutaraldehyde) and with UV light in order to create hydrogels to serve as scaffolds for cell growth. |
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+ | [[File:Scl2 Diagram.png]] | ||
[1] An, B., Kaplan, D. L., & Brodsky, B. (2014). Engineered recombinant bacterial collagen as an alternative collagen-based biomaterial for tissue engineering. Frontiers in Chemistry, 2, 40. https://doi.org/10.3389/fchem.2014.00040 | [1] An, B., Kaplan, D. L., & Brodsky, B. (2014). Engineered recombinant bacterial collagen as an alternative collagen-based biomaterial for tissue engineering. Frontiers in Chemistry, 2, 40. https://doi.org/10.3389/fchem.2014.00040 |
Revision as of 00:51, 20 October 2021
Streptococcal Collagen-Like Protein
Streptococcal Collagen-Like Protein (Scl2) was originally discovered in gram-positive S. pyogenes. It is a prokaryotic protein that can be used to mimic human collagen and has been shown to form stable triple helices[1].
Scl2 is easily expressed in E. coli and lacks the requirement for post-translational modifications; this makes it a useful alternative to recombinant human collagen expressed in eukaryotic organisms[1]. For these reasons, we chose Scl2 as the backbone for Collatrix — a collagen-mimetic gradient hydrogel for bone-soft tissue interfaces.
Scl2 can be modified to specific locations with common mammalian cell binding sites, such as fibronectin and integrin [2]. After is it produced, it can be cross-linked both chemically (with the use of glutaraldehyde) and with UV light in order to create hydrogels to serve as scaffolds for cell growth.
[1] An, B., Kaplan, D. L., & Brodsky, B. (2014). Engineered recombinant bacterial collagen as an alternative collagen-based biomaterial for tissue engineering. Frontiers in Chemistry, 2, 40. https://doi.org/10.3389/fchem.2014.00040
[2] Parenteau-Bareil, R., Gauvin, R., & Berthod, F. (2010). Collagen-Based Biomaterials for Tissue Engineering Applications. Materials, 3(3), 1863–1887. https://doi.org/10.3390/ma3031863
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 397
Illegal PstI site found at 406
Illegal PstI site found at 415
Illegal PstI site found at 469 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 397
Illegal PstI site found at 406
Illegal PstI site found at 415
Illegal PstI site found at 469 - 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 207
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 397
Illegal PstI site found at 406
Illegal PstI site found at 415
Illegal PstI site found at 469 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 397
Illegal PstI site found at 406
Illegal PstI site found at 415
Illegal PstI site found at 469
Illegal NgoMIV site found at 517
Illegal NgoMIV site found at 751
Illegal NgoMIV site found at 1230
Illegal AgeI site found at 1237 - 1000COMPATIBLE WITH RFC[1000]