Difference between revisions of "Part:BBa K3142003"
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<partinfo>BBa_K3142003 short</partinfo> | <partinfo>BBa_K3142003 short</partinfo> | ||
| − | + | Much research has verified that tripeptides initiated with a branched-chain aliphatic amino acid residue and terminated with a proline have a strong antihypertensive activity in vivo. However, it is difficult to release from their precursor proteins that are orally administered. The dipeptides FR described here may be widely used as linkers to help the release of the active peptides with proline at C-terminus from their protein precursors by ACE or gastrointestinal enzymes in human body. | |
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Revision as of 16:40, 20 October 2019
FR
Much research has verified that tripeptides initiated with a branched-chain aliphatic amino acid residue and terminated with a proline have a strong antihypertensive activity in vivo. However, it is difficult to release from their precursor proteins that are orally administered. The dipeptides FR described here may be widely used as linkers to help the release of the active peptides with proline at C-terminus from their protein precursors by ACE or gastrointestinal enzymes in human body.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]