Difference between revisions of "Part:BBa K4439002"
 
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<partinfo>BBa_K4439002 short</partinfo>
 
<partinfo>BBa_K4439002 short</partinfo>
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Recombinant Green Lacewing Silk Protein
  
 
==Abstract==
 
==Abstract==
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For the scope of our project, we designed a new recombinant silk protein N[AS]4C which adds hydrophobic protective properties to the insulative cellulose aerogel we produced, when coated on top of it. This part has been designed but not built and tested, as for the project we used the basic part ([[Part:BBa K4439001]]) to design the composite part mSA-N[AS]4C-CBD-10xHis ([[Part:BBa K4439007]]), which we successfully built and tested.
  
 
==Sequence and Features==
 
==Sequence and Features==
 
<partinfo>BBa_K4439002 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4439002 SequenceAndFeatures</partinfo>
  
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==Protein Characterization==
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*Silk proteins demonstrate interesting mechanical properties such as toughness, strength, lightweight, biodegradability and the possibility to produce different morphologies (fibers, foams, capsules, films). In addition to this, silk proteins comprise a high percentage of the amino acids glycine, serine and alanine which have an intermediate hydrophobicity.
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*Green lacewing insects produce two types of silk: one produced by the larvae (cocoon) and the other by adult females (egg-stalk). The adult produced silk acts as a protective shelter and structural support for egg stalks, which are two ideal properties for a waterproof coating for our aerogel.
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*In green lacewings, two serine- and glycine-rich silk proteins (Ma1XB1 and Ma1XB2) have been identified, both with highly repetitive core domains and small terminal domains. The core domain’s structure is rich in β-sheets with an approximative sheet-length of four amino acids between turns. These form repeating structural units constituting β-helices which have a significant positive correlation with the proteins’ surface hydrophobicity. A consensus motif for the core domain of Ma1XB2 (named [AS])had already been generated. Furthermore, a recombinant protein constituted by 8 repetitions of this [AS] module had also already been expressed in E. coli.
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*N[AS]8C’s characteristics were further tested in various morphologies such as films, capsules, hydrogels and foams. When N[AS]8C formed a film, its hydrophobic properties were enhanced.
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*Table 1 | N[AS]8C Recombinant Green Lacewing Silk Protein Characteristics
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<br>
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[[File:N-AS-8C Silk Table Characterisation.png|500px]]
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<br>
  
 
==Modeling==
 
==Modeling==
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To better see how the protein folding is, we modeled the structure of the N[AS]4C recombinant protein. One can better see the β-sheets of the core domain constituting β-helices.
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<br>
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[[File:N-AS-8C modeling.png|500px]]
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Figure 1 | 3D model of the N[AS]8C protein.
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==References==
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<ul>
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<li> Bauer, F. & Scheibel, T. (2012, 16 may). Artificial Egg Stalks Made of a Recombinantly Produced Lacewing Silk Protein. Angewandte Chemie International Edition, 51(26), 6521‑6524. https://doi.org/10.1002/anie.201200591
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<li> Bauer, F. (2013) Development of an artificial silk protein on the basis of a lacewing egg stalk protein. https://epub.uni-bayreuth.de/72/1/Diss.pdf
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</li>
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</ul>

Latest revision as of 13:42, 12 October 2022

N-[AS]8-C

Recombinant Green Lacewing Silk Protein

Abstract

For the scope of our project, we designed a new recombinant silk protein N[AS]4C which adds hydrophobic protective properties to the insulative cellulose aerogel we produced, when coated on top of it. This part has been designed but not built and tested, as for the project we used the basic part (Part:BBa K4439001) to design the composite part mSA-N[AS]4C-CBD-10xHis (Part:BBa K4439007), which we successfully built and tested.

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
    COMPATIBLE WITH RFC[1000]

Protein Characterization

  • Silk proteins demonstrate interesting mechanical properties such as toughness, strength, lightweight, biodegradability and the possibility to produce different morphologies (fibers, foams, capsules, films). In addition to this, silk proteins comprise a high percentage of the amino acids glycine, serine and alanine which have an intermediate hydrophobicity.
  • Green lacewing insects produce two types of silk: one produced by the larvae (cocoon) and the other by adult females (egg-stalk). The adult produced silk acts as a protective shelter and structural support for egg stalks, which are two ideal properties for a waterproof coating for our aerogel.
  • In green lacewings, two serine- and glycine-rich silk proteins (Ma1XB1 and Ma1XB2) have been identified, both with highly repetitive core domains and small terminal domains. The core domain’s structure is rich in β-sheets with an approximative sheet-length of four amino acids between turns. These form repeating structural units constituting β-helices which have a significant positive correlation with the proteins’ surface hydrophobicity. A consensus motif for the core domain of Ma1XB2 (named [AS])had already been generated. Furthermore, a recombinant protein constituted by 8 repetitions of this [AS] module had also already been expressed in E. coli.
  • N[AS]8C’s characteristics were further tested in various morphologies such as films, capsules, hydrogels and foams. When N[AS]8C formed a film, its hydrophobic properties were enhanced.


  • Table 1 | N[AS]8C Recombinant Green Lacewing Silk Protein Characteristics


N-AS-8C Silk Table Characterisation.png

Modeling

To better see how the protein folding is, we modeled the structure of the N[AS]4C recombinant protein. One can better see the β-sheets of the core domain constituting β-helices.


N-AS-8C modeling.png
Figure 1 | 3D model of the N[AS]8C protein.

References