Difference between revisions of "Part:BBa K143038"

Latest revision as of 13:13, 18 September 2008

SacB-EAK16-II Fusion Protein

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.

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]

Reference

1 pmid=16061392
2 pmid=16997527

</biblio>

@@ Line 2: / Line 2: @@
 <partinfo>BBa_K143038 short</partinfo>
-EAK16-II is a sixteen amino acid peptide that self-assembles to form &#946;-sheet structures in an aqueous medium. The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides <cite>1</cite>, 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.
+<br>
-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 &#945;-amylase, cystatin and interleukin-3 by B.subtilis <cite>2</cite>.
+EAK16-II is a sixteen amino acid peptide that self-assembles to form &#946;-sheet structures in an aqueous medium. The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides <cite>1</cite>, 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.
+<br>
+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 &#945;-amylase, cystatin and interleukin-3 by ''B. subtilis'' <cite>2</cite>.
+<br>
 <!-- Add more about the biology of this part here
@@ Line 23: / Line 29: @@
 #1 pmid=16061392
 #2 pmid=16997527
-#3 pmid=10974125
 </biblio>