Abstract
Head-to-sidechain macrocylic peptides, and neoglycopeptides, were readily prepared by site-specific amidation of aspartic and glutamic acid sidechain hydrazides. Hydrazides, serving as latent thioesters, were introduced through regioselective opening of the corresponding Nα-Fmoc protected anhydride precursors.
Highlights
Head-to-sidechain macrocylic peptides, and neoglycopeptides, were readily prepared by site-specific amidation of aspartic and glutamic acid sidechain hydrazides
The use of peptide Ca-thioesters as building blocks for synthetic proteins using Native Chemical Ligation (NCL) is well established.[1]. These thioesters have functioned as precursors for NCL-mediated head-to-tail peptide cyclisation.[2]. Both C-terminal thioesters and hydrazides can be readily prepared from synthetic or bacterially produced materials which, in part, overcomes the size limitations associated with traditional stepwise solid phase peptide synthesis (SPPS).[3]
Sidechain thioesters are difficult to incorporate into synthetic peptides by Fmoc-based SPPS due to their instability in the presence of piperidine
Summary
Head-to-sidechain macrocylic peptides, and neoglycopeptides, were readily prepared by site-specific amidation of aspartic and glutamic acid sidechain hydrazides. Hydrazides, serving as latent thioesters, were introduced through regioselective opening of the corresponding Na-Fmoc protected anhydride precursors.
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