Team:TU-Munich/Project/Bioaccumulation

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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 (Ref), (2) Affibodies derived from the z-domain of the antibody-binding protein A (Ref) and (3) DARPins that are based on an ankyrin scaffold. </div>
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 (Ref), (2) Affibodies derived from the z-domain of the antibody-binding protein A (Ref) and (3) DARPins that are based on an ankyrin scaffold. </div>
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====Variants of FluA====
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|Variant
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|Affinity
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|FluA
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|FluA(R95K)
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Revision as of 20:44, 30 June 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.
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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 (Ref), (2) Affibodies derived from the z-domain of the antibody-binding protein A (Ref) and (3) DARPins that are based on an ankyrin scaffold.
Text

Variants of FluA

Variant Affinity
FluA
FluA(R95K)



Glutathione S-transferase

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figure





Protein Phosphotase 1 - A molecular mop for Microcystin

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figure




References:

http://www.ncbi.nlm.nih.gov/pubmed/6327079 Edens et al., 1984

  1. http://www.ncbi.nlm.nih.gov/pubmed/6327079 Edens et al., 1984 Edens, L., Bom, I., Ledeboer, A. M., Maat, J., Toonen, M. Y., Visser, C., and Verrips, C. T. (1984). Synthesis and processing of the plant protein thaumatin in yeast. Cell, 37(2):629–33.



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