To understand how peptides may rationally be used as immunogens, we are investigating select peptide mimics for their ability to induce antibody responses that recognize a target antigen.
We have constructed a panel of peptide libraries, with emphasis on designing frameworks around the variegated residues that mimic structures on folded proteins. Such constrained peptides will give us more information about the types of structures that are required for binding (and thus for successful mimicry), as well as the chemistry of the selected amino acids. By screening the panel of peptide libraries with polyclonal antibodies against proteins of known structure, we can compare the structures of the peptide mimics we find with their corresponding protein epitopes. This gives us a good starting point for understanding the molecular basis of peptide mimicry.
For more details, visit our research lab website.
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- Breden, F, Lepik C, Longo NS, Montero M, Lipsky PE, Scott JK (2011) Comparison of antibody repertoires produced by HIV-1 infection, other chronic and acute infections, and systemic autoimmune disease. < http://www.ncbi.nlm.nih.gov/pubmed/21479208> PLoS One 6(3):316857 (11 pages)
- Watson CT, Steinberg KM, Huddleston J, Warren RL, Malig M, Schein J, Willsey AJ, Joy JB, Scott JK, Graves TA, Wilson RK, Holt RA, Eichler EE, Breden F. (2013) Am. J. Hum Genet. Complete Haplotype Sequence of the Human Immunoglobulin Heavy-Chain Variable, Diversity, and Joining Genes and Copy-Number Variation. 92(4): 530-546.