Types | DnaRegion
|
Roles | Coding
CDS
|
Sequences | BBa_K143038_sequence (Version 1)
|
Description
EAK16-II is a sixteen amino acid peptide that self-assembles to form β-sheet structures in an aqueous medium. The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides 1, triggering self-assembly when the EAK16-II peptides are exposed to physiological media or salt solution. When examined under SEM, a well-ordered nanofibre structure is formed by the association of the EAK16-II peptides and these nanofibres can futher aggregate to form a membranous 3D scaffold.
SacB is a signal peptide used in the Sec-SRP (secretory signal recognition particle) pathway by B. subtilis. Signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached) through an appropriate secretory pathway. In the case of the Sec-SRP signal peptide, they direct preproteins from the cytoplasm into the growth medium. SacB has been successfully used in the secretion of heterologous proteins such as acid-stable α-amylase, cystatin and interleukin-3 by B.subtilis 2.
Notes
BioBrick standard was applied to the SacB-EAK16-II Fusion Protein.
Source
EAK16-II is a segment from zuotin, a yeast protein. SacB was identified from the initial part of certain preprotein genes that utilises the the Sec-SRP secretory pathway 3. Both components were synthesised as a fusin protein by GeneArt.