Part:BBa_K4380000:Design

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

Design Vilnius-Lithuania Igem 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 peptide bound to a fluorescent protein, other peptide immobilized on cellulose membrane by cellulose binding domain.

Biology

The part comes from Clostridium thermocellum genomix sequence.

Figure 1: C. thermocellum cellulosome. C. thermocellum scaffoldin (CipA) contains nine type I cohesins and thus organizes a multienzyme complex that incorporates nine enzymes. The C-terminal type II dockerin of CipA binds specifically to type II cohesin modules found in cell surface proteins. Individ- ual enzymes may also adhere directly to the bacterium cell envelope by binding the single type I cohesins found in OlpA and OlpC.