Team:BrownStanfordPrinctn/Part Collection
Paper Microfluidic Collection
Our paper microfluidic parts collection has a variety of functional domains in a variety of configurations, all used to create visible hydrophobic channels on paper substrates. The collection revolves around three main functional domains- a double cellulose binding domain, a super folder GFP, and a hydrophobic domain. We have positioned these basic parts in a variety of ways, fusing them via simple flex linkers and also exploring more complicated assembly of split proteins using the complementarity of leucine zippers. This collection spans from simple to exploratory when it comes to creating a visible hydrophobic channel, and the plug and play nature of these parts open this collection up to a variety of application surrounding more generally the functionalization of cellulose, not just in a paper microfluidic context.
| Part | Description |
|---|---|
| BBa_K3260013 | Radex Domain |
| BBa_K3260014 | Flex Linker |
| BBa_K3260015 | ZE Leucine Zipper |
| BBa_K3260016 | cGFP |
| BBa_K3260017 | ZR Leucine Zipper |
| BBa_K3260018 | nGFP |
| BBa_K3260019 | dCBD + Radek Domain |
| BBa_K3260020 | dCBD + dRadek Domain |
| BBa_K3260021 | ZE + cGFP +dCBD |
| BBa_K3260022 | dRadex+ ZE+nGFP |
| BBa_K3260023 | dRadex Domain |
Peptide-Drug Collection
The peptide-drugs we synthesized had to be compatible with the workflow of the microfluidic expression and purification chips. Each of the biobricks for our drugs of choice were designed with the gene sequence of the desired protein, a His-tag, a solubility factor, and a TEV or Enterokinease cut-site for effective purification and isolation. The gene sequences of Teriparatide, hG-CSF, and Insulin were established from the literature and were optimized for expression in E. coli.
| Part | Description |
|---|---|
| BBa_K3260001 | hG-CSF with stop codon |
| BBa_K3260024 | Teriparatide with stop codon |
| BBa_K3260007 | Single chain insulin |