Team:TU-Munich/Project/Bioaccumulation

From 2013.igem.org

(Difference between revisions)
(References:)
(References:)
Line 75: Line 75:
#[[http://www.ncbi.nlm.nih.gov/pubmed/10051566 Beste et al., 1999]] Beste G, Schmidt FS, Stibora T, Skerra A. (1999) Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. ''PNAS'', 96(5):1898-903.
#[[http://www.ncbi.nlm.nih.gov/pubmed/10051566 Beste et al., 1999]] Beste G, Schmidt FS, Stibora T, Skerra A. (1999) Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. ''PNAS'', 96(5):1898-903.
#[[http://www.ncbi.nlm.nih.gov/pubmed/16307475 Vopel et al., 2005]] Vopel S, Mühlbach H, Skerra A. (2005) Rational engineering of a fluorescein-binding anticalin for improved ligand affinity. ''Biol. Chem.'', 386(11):1097-104.
#[[http://www.ncbi.nlm.nih.gov/pubmed/16307475 Vopel et al., 2005]] Vopel S, Mühlbach H, Skerra A. (2005) Rational engineering of a fluorescein-binding anticalin for improved ligand affinity. ''Biol. Chem.'', 386(11):1097-104.
-
#[[http://www.ncbi.nlm.nih.gov/pubmed/9255793 Nord et al., 1997]] Nord K, Gunneriusson E, Ringdahl J, Ståhl S, Uhlén M, Nygren PA. (1997) Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain. Nature Biotech. 15(8):772-7.
+
#[[http://www.ncbi.nlm.nih.gov/pubmed/9255793 Nord et al., 1997]] Nord K, Gunneriusson E, Ringdahl J, Ståhl S, Uhlén M, Nygren PA. (1997) Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain. ''Nature Biotech''. 15(8):772-7.
</div>
</div>

Revision as of 10:28, 12 September 2013


BioAccumulation

BioAccumulation is a possibility to remove xenobiotics from the environment by binding them to a protein that has been designed for this purpose.
Text
figure





The Fluorescein binding Anticalin FluA

There are a broad range of natural as well as engineered binding proteins availible. The most commonly known binding proteins are antibodies which defend mammals against pathogens and toxins. Beside these natural binding proteins there are more and more designed binding proteins such as (1) Anticalins based on a lipocalin scaffold [[http://www.ncbi.nlm.nih.gov/pubmed/10051566 Beste et al., 1999], [http://www.ncbi.nlm.nih.gov/pubmed/16307475 Vopel et al., 2005]], (2) Affibodies derived from the z-domain of the antibody-binding protein A (Ref) and (3) DARPins that are based on an ankyrin scaffold.

Table 1:

Variants of the fluorescein binding Anticalin FluA

Proteinvariant KD of FluA to fluorescein Literature reference BioBrick
FluA 152 nM http://www.ncbi.nlm.nih.gov/pubmed/10051566 Beste et al., 1999 <partinfo>BBa_K157004</partinfo>
FluA (R95K) 64 nM http://www.ncbi.nlm.nih.gov/pubmed/16307475 Vopel et al., 2005 not availible as BioBrick
FluA (R95K, A45I, S114T) 2 nM http://www.ncbi.nlm.nih.gov/pubmed/16307475 Vopel et al., 2005 <partinfo>BBa_K1159002</partinfo>
Text



Glutathione S-transferase

Text
Text
figure





Protein Phosphotase 1 - A molecular mop for Microcystin

Text
Text
figure




References:

  1. http://www.ncbi.nlm.nih.gov/pubmed/10051566 Beste et al., 1999 Beste G, Schmidt FS, Stibora T, Skerra A. (1999) Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. PNAS, 96(5):1898-903.
  2. http://www.ncbi.nlm.nih.gov/pubmed/16307475 Vopel et al., 2005 Vopel S, Mühlbach H, Skerra A. (2005) Rational engineering of a fluorescein-binding anticalin for improved ligand affinity. Biol. Chem., 386(11):1097-104.
  3. http://www.ncbi.nlm.nih.gov/pubmed/9255793 Nord et al., 1997 Nord K, Gunneriusson E, Ringdahl J, Ståhl S, Uhlén M, Nygren PA. (1997) Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain. Nature Biotech. 15(8):772-7.