Difference between revisions of "Part:BBa K4380000:Design"

 
(→‎Design notes)
 
(14 intermediate revisions by the same user not shown)
Line 6: Line 6:
  
  
−
===Design Notes===
+
===Design===
−
Design
+
  
 +
Vilnius-Lithuania Igem's 2022 team used this part as a novel way for peptide immobilization. The team was working to create an easily accessible nanoplastic detection tool, using peptides, whose interaction with nanoplastic particles would lead to an easily interpretable response. The system itself focused on smaller protein molecules, peptides, which are modified to acquire the ability to connect to the surface of synthetic polymers – plastics. The detection system works when peptides and nanoplastic particles combine and form a "sandwich" complex - one nanoplastic particle is surrounded by two peptides, attached to their respective protein. The sandwich complex consisted of two main parts – one is a peptide bound to a fluorescent protein, and another peptide is immobilized on a cellulose membrane by a cellulose binding domain.
  
−
 
+
===Design notes===
−
===Source===
+
The design of proteins attached to the cellulose-binding domain is relatively easy. One of the things that are important when designing a part with this domain is a linker sequence between the domain and the corresponding protein or another biomolecule.
−
 
+
The sequence of this specific cellulose binding domain came from an article by Yang et al., 2021 [1]. The authors of the article tested two cellulose binding domains and found out, that this domain can successfully be used for paper-based lateral flow immunoassays.
−
The part comes from Clostridium thermocellum genomix sequence.
+
  
 
===References===
 
===References===
 +
[1] Yang, J. M., Kim, K. R., Jeon, S., Cha, H. J., & Kim, C. S. (2021). A sensitive paper-based lateral flow immunoassay platform using engineered cellulose-binding protein linker fused with antibody-binding domains. Sensors and Actuators B: Chemical, 329, 129099. https://doi.org/10.1016/j.snb.2020.129099

Latest revision as of 16:59, 13 October 2022


Cellulose Binding domain (CBD)


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]


Design

Vilnius-Lithuania Igem's 2022 team used this part as a novel way for peptide immobilization. The team was working to create an easily accessible nanoplastic detection tool, using peptides, whose interaction with nanoplastic particles would lead to an easily interpretable response. The system itself focused on smaller protein molecules, peptides, which are modified to acquire the ability to connect to the surface of synthetic polymers – plastics. The detection system works when peptides and nanoplastic particles combine and form a "sandwich" complex - one nanoplastic particle is surrounded by two peptides, attached to their respective protein. The sandwich complex consisted of two main parts – one is a peptide bound to a fluorescent protein, and another peptide is immobilized on a cellulose membrane by a cellulose binding domain.

Design notes

The design of proteins attached to the cellulose-binding domain is relatively easy. One of the things that are important when designing a part with this domain is a linker sequence between the domain and the corresponding protein or another biomolecule. The sequence of this specific cellulose binding domain came from an article by Yang et al., 2021 [1]. The authors of the article tested two cellulose binding domains and found out, that this domain can successfully be used for paper-based lateral flow immunoassays.

References

[1] Yang, J. M., Kim, K. R., Jeon, S., Cha, H. J., & Kim, C. S. (2021). A sensitive paper-based lateral flow immunoassay platform using engineered cellulose-binding protein linker fused with antibody-binding domains. Sensors and Actuators B: Chemical, 329, 129099. https://doi.org/10.1016/j.snb.2020.129099