Abstract:
:The development of rational methods to design 'continuous' sequence mimetics of discontinuous regions of protein sequence has, to now, been only marginally successful. This has been largely due to the difficulty of constraining the recognition elements of a mimetic structure to the relative conformational and spatial orientations present in the parent molecule. Using peptide mapping to determine 'active' antigen recognition residues, molecular modeling, and a molecular dynamics trajectory analysis, we have developed a peptide mimic of an anti-CD4 antibody, containing antigen contact residues from multiple CDRs. The design described is a 27-residue peptide formed by juxtaposition of residues from 5 CDR regions. It displays an affinity for the antigen (CD4) of 0.9nM, compared to 2nM for the parent antibody ST40. Nevertheless, the mimetic shows low biological activity in an anti-retroviral assay.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Casset F,Roux F,Mouchet P,Bes C,Chardes T,Granier C,Mani JC,Pugnière M,Laune D,Pau B,Kaczorek M,Lahana R,Rees Adoi
10.1016/s0006-291x(03)01131-8subject
Has Abstractpub_date
2003-07-18 00:00:00pages
198-205issue
1eissn
0006-291Xissn
1090-2104pii
S0006291X03011318journal_volume
307pub_type
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