Azide‐rich peptides via an on‐resin diazotransfer reaction

Abstract

Azide-containing amino acids are valuable building blocks in peptide chemistry, because azides are robust partners in several bioorthogonal reactions. Replacing polar amino acids with apolar, azide-containing amino acids in solid-phase peptide synthesis can be tricky, especially when multiple azide residues are to be introduced in the amino acid sequence. We present a strategy for effectively incorporating multiple azide-containing residues site-specifically.

Bundle-forming α-helical peptide–dendron hybrid

“…11 Because of the simplicity of the design and compact size of the peptides, a family of α-helical “LK” peptides has been developed as self-assembling modules for biomaterials. 12 Starting from an amino acid sequence similar to these α-helical “LK” peptides, 13 we replaced two surface lysine residues with residues bearing water-soluble poly(alkyl ether) dendrons in the side chain.…”

Peptide–dendron hybrids that adopt sequence-encoded β-sheet conformations

“…The same polar and non-polar residues were used in our previously reported α-helical bundle-forming peptide-dendron hybrids. 32, 33, 54, 55 The side-chain amino group of each lysine residue is efficiently acylated using dendritic pentafluorophenyl esters. 54 DeGrado and Lear have shown that a seven-residue peptide with alternating leucine and lysine residues self-assembles into a β-sheet structure in buffered aqueous solution.…”

“…Rudimentary protein design rules offer a foundation from which to construct functional materials via programmable hierarchical organization of peptide-dendron hybrids. The recent report of self-organizable α-helix bundle-forming peptide-dendron hybrids 32, 33, 54, 55 is a promising starting point because natural helix bundles exhibit diverse functionality. 67, 68 Indeed, functional hybrid materials based on α-helix bundle-forming peptide-polymer conjugates have validated the concept of designing binding sites for light-harvesting chromophores in polymeric films.…”

“…Inspired by the tunability and processability afforded by combinations of peptides with dendrons, we have investigated hybrids of dendrons with an α-helical bundle-forming peptide. 32, 33, 54, 55 The defined arrangement of different amino acids in the core of an α-helix bundle motif could allow us to synthesize chemical gradients or unique binding sites within supramolecular dendrimers. We recently reported examples of α-helix bundle-forming peptide-dendron hybrids that self-organize in an hexagonally ordered array of columns.…”

Application of multicomponent reactions in the total synthesis of natural peptides

“…5 Peptides as highly attractive molecular structures have played key roles in biological research and therapeutic applications and they possess a wide range of physiological and cellular functions. [6][7][8] Advances in this regard are due to discovery of solid-supported synthesis 9,10 and the development of reagents and methods for direct amide formation. 7 Nevertheless, novel methods for the rapid production of these biopolymers are constantly being explored.…”