Abstract: Peptide analogs formed by replacing one or more, but not all, amino acids of a peptide chain with 1,2-dihydro-3(6H)-pyridinone, display an unusually strong tendency to assume a &bgr;-strand conformation and to enter into &bgr;-sheet-like interactions with peptides and other peptide analogs that engage in &bgr;-sheet-like interactions with peptides. The peptide analogs of this invention therefore have utility has &bgr;-strand mimics offering advantages over native peptides as well as &bgr;-strand mimics of the prior art.

Abstract: A method for detecting cyclization of acyclic compounds is disclosed. In particular, the invention relates to a method of screening for macrocyclic peptidase inhibitors, and is useful for screening a combinatorial library of compounds.

Abstract: Peptoids are provided which are polymers comprised of monomer units wherein the monomer units include at least some substitute amino acids and may include conventional amino acids. The peptoids can be synthesized in large numbers so as to provide libraries of peptoids which can be screened in order to isolate peptoids of desired biological activity. Although the peptoids may include amino acids, they preferably include only substituted amino acids and are designed in a manner so as to have a particular biological activity. Certain peptoids are designed to mimic as closely as possible the activity of known proteins. Other peptoids are designed so as to have greater or lesser activity than known proteins and may be designed so as to block known receptor sites and/or elicit a desired immunogenic response and thereby act as vaccines. In that the peptoids are comprised of substitute amino acids they can be designed to have structures which natural proteins cannot conform to.

Abstract: Peptoids are provided which are polymers comprised of monomer units wherein the monomer units include least some substitute amino acids and may include conventional amino acids. The peptoids can be synthesized in large numbers so as to provide libraries of peptoids which can be screened in order to isolate peptoids of desired biological activity. Although the peptoids may include amino acids, they preferably include only substituted amino acids and are designed in a manner so as to have a particular biological activity. Certain peptoids are designed to mimic as closely as possible the activity of known proteins. Other peptoids are designed so as to have greater or lesser activity than known proteins and may be designed so as to block known receptor sites and/or elicit a desired immunogenic response and thereby act as vaccines. In that the peptoids are comprised of substitute amino acids they can be designed to have structures which natural proteins cannot conform to.

Abstract: Mixtures of peptoids are provided. The subject peptoid mixtures comprise at least five non-homopolymeric polymers of differing sequences having a selected number of monomer units. The polymers of the subject mixtures are preferably selected from the group of compounds of the general formula: X.sub.a --(NR--CH.sub.2 --CO).sub.n --X.sub.b, X.sub.a --(O--CHR--CO).sub.n --X.sub.b, X.sub.a --(NH--CHR--CS).sub.n --X.sub.b, X.sub.a --(NOH--CHR--CO).sub.n --X.sub.b, X.sub.a --(O--CHR--CH.sub.2 --CO).sub.n --X.sub.b, X.sub.a --(NH--CHR--CH.sub.2 --SO.sub.2).sub.n --Xb, Xa--(NR--CH.sub.2 CH.sub.2 --SO.sub.2).sub.n --X.sub.b, X.sub.a --(NR--CH.sub.2 CH.sub.2 --NHCO).sub.n --X.sub.b and X.sub.a --(NR--CH.sub.2 CH.sub.2 --OCO).sub.n X.sub.b, where each R is independently a side chain capable of interaction with a protein, carbohydrate, lipid or nucleic acid; n is an integer from 2 to 50, inclusive; and X.sub.a and X.sub.

Abstract: A variety of chemical reactions are rate enhanced by the use of antibodies whose antibody binding sites are complementary to the reactant orientations or transition states which lead to the desired product. The reactions include pericyclic reactions such as Claisen and Cope rearrangements and Diels Alder reactions, peptide bond hydrolysis reactions, peptide fragment ligations, lactonizations and cyclic peptide syntheses, glycosylations, aldol additions, nucleoside syntheses and transesterification reactions. Haptens which are stable analogues of unstable transition states, or which are analogues of desired products, in some cases with leaving groups still attached for purposes of avoidance of product inhibition, are used to generate the antibodies.

Abstract: Compounds are provided that are useful in inhibiting cysteine or serine proteinases. The compounds define a peptide backbone with a sulfur atom substituted in the backbone. A leaving group is associated, or bonded, to a carbon atom adjacent to the sulfur atom. The leaving group is displaceable either by hydrolysis under physiological conditions (with the hydrolyzed compound forming an aldehyde enzyme inhibitor) or by an active-site nucleophile of a cysteine or serine proteinase. When the leaving group is displaced by hydrolysis, then the compound functions as a protected derivative of the aldehyde functional group and is stabilized against oxidation or degradation, yet allows for release of the aldehyde moiety at the pharmacological site of action. The peptide sulfide analogues bearing a leaving group displaced by the active-site nucleophile covalently bond cysteine or serine proteinases and thus irreversibly inhibit these enzymes.

Abstract: The crosslinking agent contains an acylhydrazide moiety, through which it is linked to a cytosine residue on the first chain; and an .alpha.-haloketal moiety which, after attachment of the crosslinking agent to the first chain, is hydrolyzed to an .alpha.-haloketone moiety, through which linking is effected to the base-paired guanine residue on the second chain.

Abstract: Estrogenic steroids are synthesized by combining under conditions favoring the formation of a trans-olefin, a .gamma.-arylpropanal with a 5,5,8,8-tetraalkoxy Wittig reagent. After hydrolysis of the gem-diethers, the resulting dioxo is internally condensed to form a cyclopentenone. The ketone is reduced to an oxy group and the resulting 2-(6'-arylhex-3'-enyl-1)cyclopent-2-en-1-ol or derivative thereof is cyclized to the .DELTA..sup.13,17 -estrene, preferably 17-alkyl-.DELTA..sup.13,17 -estrene with the A ring aromatized. After epoxidation, the 17-alkyl derivative is rearranged to form the 13-alkyl-1,3,5(10)-estratien-17-one. New compounds are provided as intermediates and final products.