@article {Che:January 2008:1472-8222:101,
	author = "Che, Ye",
	author = "Marshall, Garland R",
	title = "Privileged scaffolds targeting reverse-turn and helix recognition",
	journal = "Expert Opinion on Therapeutic Targets",
	volume = "12",
	year = "January 2008",
	abstract = "<I>Background</I>: Protein-protein interactions dominate molecular recognition in biologic systems. One major challenge for drug discovery arises from the very large surfaces that are characteristic of many protein-protein interactions. <I>Objectives</I>: To identify `drug-like' small molecule leads capable of modulating protein-protein interactions based on common protein-recognition motifs, such as &#945;-helices, &#946;-strands, reverse-turns and polyproline motifs for example. <I>Overview</I>: Many proteins/peptides are unstructured under physiologic conditions and only fold into ordered structures on binding to their cellular targets. Therefore, preorganization of an inhibitor into its protein-bound conformation reduces the entropy of binding and enhances the relative affinity of the inhibitor. Accordingly, this review describes a general strategy to address the challenge based on the `privileged structure hypothesis' [Che, PhD thesis, Washington University, 2003] that chemical templates capable of mimicking surfaces of protein-recognition motifs are potential privileged scaffolds as small-molecule inhibitors of protein-protein interactions. The authors highlight recent advances in the design of privileged scaffolds targeting reverse-turn and helical recognition. <I>Conclusions</I>: Privileged scaffolds targeting common protein-recognition motifs are useful to help elucidate the receptor-bound conformation and to provide non-peptidic, bioavailable substructures suitable for optimization to modulate protein-protein interactions.",
	pages = "101-114(14)",
	url = "http://www.ingentaconnect.com/content/apl/ett/2008/00000012/00000001/art00009"
	doi = "doi:10.1517/14728222.12.1.101"
}