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Affimer
An Affimer is a small, highly stable protein engineered to display peptide loops which provide a high affinity binding surface for a specific target protein. It is a protein of low molecular weight, 12–14 kDa, derived from the cysteine protease inhibitor family of cystatins.
Affimer proteins are composed of a scaffold, which is a stable protein based on the cystatin protein fold. They display two peptide loops and an N-terminal sequence that can be randomised to bind different target proteins with high affinity and specificity similar to antibodies. Stabilisation of the peptide upon the protein scaffold constrains the possible conformations which the peptide may take, thus increasing the binding affinity and specificity compared to libraries of free peptides.
==Structure and generation==
Affimer proteins were developed initially at the MRC Cancer Cell Unit in Cambridge then across two laboratories at the University of Leeds.〔〔〔〔 They are derived from cystatin proteins,〔(【引用サイトリンク】url=https://www.avactalifesciences.com/2014/05/22/affimers-next-generation-affinity-reagents/ )〕 which function in nature as cysteine protease inhibitors, and share the common tertiary structure of an alpha-helix lying on top of an anti-parallel beta-sheet. These non-antibody scaffold proteins were engineered to be stable, non-toxic, biologically neutral and contain no post-translational modifications or disulphide bridges. Affimer technology makes use of two separate loop sequences, incorporating a total of 12 to 36 amino acids, to create a large potential target interaction surface of 650 to 1000 Å2, allowing for highly-specific, high affinity binding to target proteins.〔〔 Consequently, Affimer molecules can distinguish between proteins that differ by only a single amino acid, can detect subtle changes in protein expression levels even in a multiplexed format and can distinguish between multiple closely related protein domains. Phage display libraries of 1010 randomised potential target interaction sequences are generated and screened to identify the Affimer with high-specificity binding to the target protein and binding affinities in the nM range. The use of ''in vitro'' screening techniques allows affinity maturation to be performed to achieve even greater binding affinities and means that the target space is not limited by an animal host’s immune system. Affimer reagents have been produced to a large number of targets including ubiquitin chains,〔(【引用サイトリンク】title=Anti-diUbiquitin K48-linkage Affimer (36-28) )〕 immunoglobulins〔(【引用サイトリンク】title=Anti-Immunoglobulin Research Area of Affimers )〕 and C-reactive protein, for use in a number of molecular recognition applications.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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