Abstract

The authors have recently focused on the design of TASP mols. of 4a-helix bundle topol., in which antigenic helical segments of protein surface domains are assembled on suitable templates. Here, in a first approach, the native sequence 58-74 of the a1 heavy chain domain of HLA-A2 was modeled in order to increase helix stability and amphiphilicity of the 17-mer peptide, preserving the residues for pot. T-cell receptor binding properties. [on SciFinder (R)]

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