The design of peptides to generate antibodies against protein epitopes is still considered an art. However, experienced researchers can use an educated approach for the design of immune response inducing peptide sequences for example by determining the amino acid sequence regions exposed to the surface of a protein. One approach is to review the folding of proteins and to search for β-turn loops where the amino acid residues at the turns are pointed to the surface of the proteins. This approach works well for proteins for which the 3D structures are available in a public data base such as the Pubmed Structure database [http://www.ncbi.nlm.nih.gov/structure/] or the RCSB PDB database [http://www.rcsb.org/pdb/home/home.do]. Another approach is to screen the protein sequences for sequence regions that have a high probability to induce immunization using bioinformatic methods. The following web link can help to achieve this:
The multiple antigen peptides (MAP) system represents another approach to anti-peptide antibody elicitation. It has been reported that MAPs can be used for the production of high-titer anti-peptide antibodies as well as synthetic peptide vaccines. The system was first described by Dr. James Tam. A MAP contains a small immunologically inert core molecule of radially branched lysines dendrites onto which a number of peptide antigens are anchored. The result is a large macromolecule which has a high molar ratio of peptide antigen to core molecules and does not require further conjugation to a carrier protein. The α- and ε-amino functional groups of lysine residues are used to form a dendrimeric type core to which multiple peptide chains are attached. Depending on the number of lysines used to synthesize the core structure different numbers of peptide branches can be synthetically attached.
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