Revision as of 23:39, 6 March 2013

Overview

Protein binding

==Antikörper==
==Affibody==

Affibody Z-EGFR-1907

(BBa_K404302)

Affibodies are small (6 kDa), soluble high-affinity proteins. They are derived from the IgG-binding B domain of the Staphylococcal protein A, which was engineered to specifically bind to certain peptides or proteins. This so-called Z domain consists of an antiparallel three-helix bundle and is advantageous due to its proteolytic and thermodynamic stability, its good folding properties and the ease of production via recombinant bacteria (Nord et al., 1997). Affibodies can be used for example for tumor targeting (Wikman et al., 2004) and diagnostic imaging applications (Orlova et al., 2006; Orlova et al., 2007). The ZEGFR:1907 Affibody was engineered to specifically bind the EGF receptor with an affinity determined to be KD = 2.8 nM (Friedman et al., 2008). The EGF receptor is overexpressed in certain types of tumors, e.g. in breast (Walker & Dearing, 1999), lung (Hirsch et al., 2003) and bladder (Colquhoun & Mellon, 2002) carcinomas, and is therefore a suitable target for cancer imaging or therapeutic applications. Because of their good tumor uptake, and their property to become internalized into the target cells with an efficiency of 19 – 24% within one hour – compared to 45% of the natural ligand EGF - the ZEGFR:1907 Affibody was chosen for therapeutic applications by the Freiburg iGEM Team 2010 (Friedman et al., 2008; Göstring et al., 2010). ==Darpin==

Anticalin

The Anticalin technology was developed by Prof. Dr. A. Skerra (TU Munich, Germany) that are based on lipocalins The anticalins availible as BioBricks are the digoxigenin binding anticalin DigA (BBa_K243003) and the fluorescein binding anticalin FluA (BBa_K157004).

Small molecule binding

Fluoreszein Digitonin

Sugar binding

Cellulose Binding

@@ Line 2: / Line 2: @@
 =Protein binding=
-Antikörper<br>
+==Antikörper==<br>
-Affibody<br>
+==Affibody==<br>
-Darpin<br>
+ Affibody Z-EGFR-1907
+(BBa_K404302)
+Affibodies are small (6 kDa), soluble high-affinity proteins. They are derived from the IgG-binding B domain of the Staphylococcal protein A, which was engineered to specifically bind to certain peptides or proteins. This so-called Z domain consists of an antiparallel three-helix bundle and is advantageous due to its proteolytic and thermodynamic stability, its good folding properties and the ease of production via recombinant bacteria (Nord et al., 1997). Affibodies can be used for example for tumor targeting (Wikman et al., 2004) and diagnostic imaging applications (Orlova et al., 2006; Orlova et al., 2007). The ZEGFR:1907 Affibody was engineered to specifically bind the EGF receptor with an affinity determined to be KD = 2.8 nM (Friedman et al., 2008). The EGF receptor is overexpressed in certain types of tumors, e.g. in breast (Walker & Dearing, 1999), lung (Hirsch et al., 2003) and bladder (Colquhoun & Mellon, 2002) carcinomas, and is therefore a suitable target for cancer imaging or therapeutic applications. Because of their good tumor uptake, and their property to become internalized into the target cells with an efficiency of 19 – 24% within one hour – compared to 45% of the natural ligand EGF - the ZEGFR:1907 Affibody was chosen for therapeutic applications by the Freiburg iGEM Team 2010 (Friedman et al., 2008; Göstring et al., 2010).
+==Darpin==<br>
+==Anticalin==
 The Anticalin technology was developed by Prof. Dr. A. Skerra (TU Munich, Germany) that are based on lipocalins
 The anticalins availible as BioBricks are the digoxigenin binding anticalin DigA (<partinfo>BBa_K243003</partinfo>) and the fluorescein binding anticalin FluA (<partinfo>BBa_K157004</partinfo>).

Difference between revisions of "Ligand Binding"