Difference between revisions of "Part:BBa K3351008"
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===Summary=== | ===Summary=== | ||
PhaP is the dominant protein naturally attached on the surface of the PHA granules. This protein contains a hydrophobic granule binding domain and a cytosol-facing hydrophilic domain. PhaP-tagged proteins could interact with various types of hydrophobic surfaces. So PhaP is an effective anchor to hydrophobic polymer surface for surface functionalization. PhaP allows a more flexible display of AMP on the biomaterial surface and demonstrates its efficacy for wound healing. | PhaP is the dominant protein naturally attached on the surface of the PHA granules. This protein contains a hydrophobic granule binding domain and a cytosol-facing hydrophilic domain. PhaP-tagged proteins could interact with various types of hydrophobic surfaces. So PhaP is an effective anchor to hydrophobic polymer surface for surface functionalization. PhaP allows a more flexible display of AMP on the biomaterial surface and demonstrates its efficacy for wound healing. | ||
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Latest revision as of 14:03, 19 October 2020
PhaP, amphiphilic polyhydroxyalkanoates (PHAs)-granule-associated protein.
Summary
PhaP is the dominant protein naturally attached on the surface of the PHA granules. This protein contains a hydrophobic granule binding domain and a cytosol-facing hydrophilic domain. PhaP-tagged proteins could interact with various types of hydrophobic surfaces. So PhaP is an effective anchor to hydrophobic polymer surface for surface functionalization. PhaP allows a more flexible display of AMP on the biomaterial surface and demonstrates its efficacy for wound healing.
Reference
[1] Xue Q, Liu XB, Lao YH, Wu LP, Wang D, Zuo ZQ, Chen JY, Hou J, Bei YY, Wu XF, Leong KW, Xiang H, Han J. Anti-infective biomaterials with surface-decorated tachyplesin I. Biomaterials. 2018 Sep;178:351-362. doi: 10.1016/j.biomaterials.2018.05.008. Epub 2018 May 9. PMID: 29778319.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]