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note
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We determined the necessary coupling conditions of the tert-butyl ester of D-Lac compared to normal amino acids by synthesis of a model peptide sequence on p-methyl-benzyldryl-amine (MBHA) resin. The free amino function of this resin was transformed with the help of Z-Glu(OtBu) into a carboxylate function allowing an analogous N to C solid-phase peptide-synthesis protocol like in the combinatorial library. The only difference is the higher acid sensitivity of the MBHA resin compared to TentaGel. It also allows the cleavage of the C-terminal tert-butyl esters with 50% TFA. In addition, the synthesized peptide can be cleaved with trifluoromethane sulfonic acid (TFMSA; 10% in TFA) and then analyzed with NMR spectroscopic techniques. These tests showed that it is possible to use the same conditions as those for like for amino acids to guarantee the quantitative coupling of D-Lac.
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33746287120
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note
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However, the latter can not be used here as it does not swell in aqueous solutions and hence does not allow subsequent on-bead binding studies in water. For this purpose the hydrophilic TentaGel is the best choice.
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