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Efficient method for the preparation of peptoids [oligo(N-substituted glycines)] by submonomer solid-phase synthesis
Oligomers of N-substituted glycines, or “peptoids“, represent a new class of polymers (Figure 1) that are not found in nature, but are synthetically accessible and have been shown to possessExpand
Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors.
This discriminatory mechanism explains how SH3 and WW protein interaction domains achieve specific but low-affinity recognition, a property that is necessary for transient signaling interactions, and can be exploited. Expand
NMR determination of the major solution conformation of a peptoid pentamer with chiral side chains.
Experimental and theoretical studies of the structural properties of chiral peptoids lay the groundwork for the rational design of more complex polypeptoid molecules, with a variety of applications, ranging from nanostructures to nonviral gene delivery systems. Expand
In vitro self-assembly of tailorable nanotubes from a simple protein building block
High-resolution detail of the ring–ring interface allowed the selection of sites for specific cysteine mutations capable of engaging in disulfide bond formation across rings, thereby generating stable Hcp1 nanotubes. Expand
Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides
The in vitro activities of ampetoids are strikingly similar to those of AMPs themselves, suggesting a strong mechanistic analogy, and add to the growing evidence that nonnatural foldamers will emerge as an important class of therapeutics. Expand
Sequence-specific polypeptoids: a diverse family of heteropolymers with stable secondary structure.
A family of structured oligo-N-substituted-glycines (peptoids) up to 36 residues in length is synthesized and characterized by using an efficient solid-phase protocol to incorporate chemically diverse side chains in a sequence-specific fashion. Expand
Peptoids: a modular approach to drug discovery.
Peptoids, oligomers of N-substituted glycines, are described as a motif for the generation of chemically diverse libraries of novel molecules and peptide ligands of three biological systems were found with affinities comparable to those of the corresponding peptides. Expand
Proteolytic studies of homologous peptide and N-substituted glycine peptoid oligomers
Abstract Homologous L-amino acid, D-amino acid, and parallel and anit-parallel (retro) sequence N-substituted glycine peptide and peptoid oligomers were prepared and incubated with proteases fromExpand
Comparison of the proteolytic susceptibilities of homologous L‐amino acid, D‐amino acid, and N‐substituted glycine peptide and peptoid oligomers
A series of homologous L‐amino acid, D‐amino acid, and both parallel and anti‐parallel (retro) sequence N‐substituted glycine peptide and peptoid oligomers were prepared and incubated with a seriesExpand