In order to obtain the best results for the production of antibodies, it is necessary to carefully design the antigen peptide . The design should meet a basic condition: during the immunization process, the antigen will not produce an excessive immune response, but at the same time produce a pair. The protein of interest has an antibody that binds. Although antigenic peptide design is a very complex topic, http:// there are several key basic design principles that can be provided for your reference:
1. Determining the use of the antibody (application) It is necessary to develop a new research project to clarify some basic characteristics of the protein of interest, especially if the structure of the protein is known to be accessible to the selected antibody. great help. However, in the absence of such precise structural information (most of which is the case), understanding the use (application) of the study can affect the strategy of polypeptide design. For example, if the focus of the study is on different regions of the protein, such as the C- terminus or the N- terminus, or proteins in a particular state, such as phosphorylation, then the peptides designed according to the desired sequence and the corresponding antibodies produced are There should be no difficulty in application, however, the conformation of the protein will affect the interaction between the antibody and its recognition region. A problem that may exist in this case is that if the recognition region is hidden inside the protein in the folded protein, the antibody will not be able to reach the region. (cannot create interaction).
2 , the selection principle of the identification area Generally speaking, the most ideal antigenic recognition area should be hydrophilic, located on the surface of the protein and structurally easy to deform. Because in most natural (natural) environments, hydrophilic regions tend to concentrate on the surface of the protein, and hydrophobic regions are often entrapped inside the protein. Similarly, antibodies can only interact with recognition regions found on the surface of the protein. When these recognition regions have sufficient structural deformability and are transferred to a position where the antibody can be contacted, there is a high affinity with the antibody.
3. A region continuous with a discontinuous recognition region refers to an recognition region composed of a continuous amino acid sequence (residue). Most antibodies are directed against a continuous recognition region, and the ability of antibodies to bind to such regions with high affinity indicates that the sequence is not inside the protein. A discontinuous recognition region is a segment of a polypeptide that represents a certain fold, or an identification region of an antibody that links two separate polypeptides together. In some cases, antibodies against such discrete recognition regions can also be produced, except that the antigenic peptide used for immunization must have a secondary structure similar to the discontinuous recognition region, and the length of the sequence needs to meet the relevant requirements.
4. Basic recommendations In order to avoid the risk of the recognition region being hidden inside the protein, we usually recommend selecting the corresponding antibodies produced by the N and C ends of the protein. Because in intact proteins, both ends of N and C are usually exposed to the surface of the protein. However, it is important to note that the C- terminal hydrophobicity of membrane proteins is too strong to be suitable as an antigen.
5 , the length of the sequence Usually we recommend the antigen peptide sequence length between 8-20 amino acid residues, if too short, the polypeptide is too specific, the affinity between the antibody produced and the natural protein (binding ability) is not enough Strong risk, too, if the sequence length exceeds 20 , it is possible to introduce a secondary structure, the resulting antibody loses the possibility of specificity, and the longer the peptide chain, the more difficult the synthesis is, and it is difficult to obtain a high-purity product.
6 , the choice of carrier protein cross-linking
Basic principles: the end remote from the carrier protein is added to the antibody recognition region, Cys is the preferred method of crosslinking in the absence of N or C-terminus in the sequence Cys plus case.
7. Common analysis software MacVecfor TM ; DNA star TM ; PC-Gene TM .
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