Abstract
We report a simple reductive amination protocol to ligate two peptides, while simultaneously installing a β-turn mimic at the ligation junction. This strategy uses commercially available materials, mild chemical conditions, and a chemoselective ligation reaction of unprotected peptide substrates accessed through standard solid phase methods. This system was implemented in a designed β-hairpin system, and biophysical analysis demonstrates effective mimicry of the β-turn.
Highlights
We report a simple reductive amination protocol to ligate two peptides, while simultaneously installing a β-turn mimic at the ligation junction
In some cases it has been suggested that the residual functionality can act as a mimic of an amide bond;[3] there are as yet no reports in the literature of a ligation junction being designed to act as a mimic of a larger element of protein structure
TrpZip[1] has been extensively characterized in terms of its 3D structure and thermodynamics of folding, and has been shown to contain a β-turn, modification of which can alter the stability of the peptide fold
Summary
We report a simple reductive amination protocol to ligate two peptides, while simultaneously installing a β-turn mimic at the ligation junction. We present a simple and synthetically accessible ligation junction that enables the rapid and highyielding chemical ligation of two peptide fragments, and which in doing so forms a mimic of a β-turn. TrpZip[1] has been extensively characterized in terms of its 3D structure and thermodynamics of folding, and has been shown to contain a β-turn, modification of which can alter the stability of the peptide fold.
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