Difference between revisions of "Part:BBa K3712020"

 
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<partinfo>BBa_K3712020 short</partinfo>
 
<partinfo>BBa_K3712020 short</partinfo>
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===USAGE AND BIOLOGY===
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<p>TLR2 antagonist is the binding sites of TLR2 to triacylated lipoproteins, which can inhibit P.acnes surface antigen by binding to it, preventing it from binding to TLR2 on the cell surface and avoiding inflammation. We intercepted TLR2 antagonist from TLR2 and performed some site-directed mutations. The first is to shorten the beta loop to prevent triacylated lipoproteins from missing the target. Secondly, the hydrophobicity of the hydrophobic pocket was enhanced to improve the binding ability of lipoprotein. In this way, we expect to obtain an effective TLR2 antagonist with significant anti-inflammatory effects.</p>
  
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LR2 antagonist is the binding sites of TLR2 to triacylated lipoproteins, which can inhibit P.acnes surface antigen by binding to it, preventing it from binding to TLR2 on the cell surface and avoiding inflammation. We intercepted TLR2 antagonist from TLR2 and performed some site-directed mutations. The first is to shorten the beta loop to prevent triacylated lipoproteins from missing the target. Secondly, the hydrophobicity of the hydrophobic pocket was enhanced to improve the binding ability of lipoprotein. In this way, we expect to obtain an effective TLR2 antagonist with significant anti-inflammatory effects.
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===Future direction:===
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<p>A purer Wild-type/Optimized TLR2 antagonist should be obtained through molecular sieve and concentrated to conduct ITC experiment.</p>
  
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===Usage and Biology===
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Revision as of 08:08, 21 October 2021


Wild-type TLR2 antagonist

USAGE AND BIOLOGY

TLR2 antagonist is the binding sites of TLR2 to triacylated lipoproteins, which can inhibit P.acnes surface antigen by binding to it, preventing it from binding to TLR2 on the cell surface and avoiding inflammation. We intercepted TLR2 antagonist from TLR2 and performed some site-directed mutations. The first is to shorten the beta loop to prevent triacylated lipoproteins from missing the target. Secondly, the hydrophobicity of the hydrophobic pocket was enhanced to improve the binding ability of lipoprotein. In this way, we expect to obtain an effective TLR2 antagonist with significant anti-inflammatory effects.

Future direction:

A purer Wild-type/Optimized TLR2 antagonist should be obtained through molecular sieve and concentrated to conduct ITC experiment.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 178