The exploration of privileged structures in drug discovery is a rapidly emerging theme in
medicinal chemistry. These structures represent a class of molecules capable of binding to …

The breadth of structure and function displayed by the molecules of biology is remarkable.
Considering that there are only three major biopolymer backbones (proteins, ribonucleic …

A protein in its native, folded conformation creates a solvent-exposed (exterior) surface and
a solventexcluded (interior) surface (Figure 1). Enzyme active sites are most often found at …

Among the strategies that can lead to the discovery of new drugs, the identification and use
of privileged structures, molecular fragments that are able to interact with more than one …

Substantial progress has been made in the synthesis and characterization of various
oligomeric molecules capable of autonomous folding to well-defined, repetitive secondary …

The achiral backbone of oligo-N-substituted glycines or “peptoids” lacks hydrogen-bond
donors, effectively preventing formation of the regular, intrachain hydrogen bonds that …

Oligomeric N-substituted glycines or “peptoids” with α-chiral, aromatic side chains can adopt
stable helices in organic or aqueous solution, despite their lack of backbone chirality and …

Nonpeptidic foldamers capable of displaying protein-like functionality were prepared by
swapping amide bonds with 1, 2, 3-triazole rings. The overall conformation of these triazole …

The simplest peptide structural element is the peptide β-strand. The β-strand is a linear or
sawtoothed arrangement of amino acids with amide bonds being almost coplanar, side …

Molecules that fold to mimic protein secondary structures have emerged as important targets
of bioorganic chemistry. Recently, a variety of compounds that mimic helices, turns, and …