title: Chemogenomics with protein secondary-structure mimetics.
abstract: During molecular recognition of proteins in biological systems, helices, reverse turns, and beta-sheets are dominant motifs. Often there are therapeutic reasons for blocking such recognition sites, and significant progress has been made by medicinal chemists in the design and synthesis of semirigid molecular scaffolds on which to display amino acid side chains. The basic premise is that preorganization of the competing ligand enhances the binding affinity and potential selectivity of the inhibitor. In this chapter, current progress in these efforts is reviewed.
authors.affiliation: Department of Biochemistry, Washington University, St. Louis, MO, USA.
authors.forename: Garland R
authors.initials: GR
authors.lastname: Marshall
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Kuster
authors.forename: Ye
authors.initials: Y
authors.lastname: Che
mesh_terms: D001665:Binding Sites; D040761:Biomimetic Materials / Q000737:chemistry*; D015195:Drug Design; D023281:Genomics; D008024:Ligands; D008958:Models, Molecular; D008967:Molecular Biology / Q000379:methods; D025941:Protein Interaction Mapping; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D040901:Proteomics; D013816:Thermodynamics
chemical_list: D008024:Ligands; D011506:Proteins