Team:TU-Munich/Project/Bioaccumulation
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==BioAccumulation== | ==BioAccumulation== | ||
- | <div class="box-center">BioAccumulation is a possibility to remove xenobiotics from the environment by binding them to a protein that has been designed for this purpose.</div> | + | <div class="box-center"> |
+ | [[File:TUM13 Physco-lifecycle.png|thumb|right|350px| Figure 1: General principle of BioAccumulation]] | ||
+ | BioAccumulation is a possibility to remove xenobiotics from the environment by binding them to a protein that has been designed for this purpose.</div> | ||
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== The Fluorescein binding Anticalin FluA== | == 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. | 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. |
Revision as of 08:26, 13 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.
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> |
Glutathione S-transferase
Text
Protein Phosphotase 1 - A molecular mop for Microcystin
Text
References:
- 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/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.
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