Abstract
The backbone amide linker strategy, in which the growing peptide chain is anchored to a solid support via a backbone amide nitrogen, has proven to be successful for the synthesis of cyclic peptides. Optimisation of the reaction conditions for the synthesis of c(Gly-Trp-βAla-Phe) could be accomplished by the help of high resolution magic angle spinning (HR MAS) NMR and the results are presented here. Signal vanishing of HR MAS NMR resonances were encountered and proven to be originated from interchain aggregations of peptide chains.
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