Abstract: Dimeric oligopeptide mixture sets, their synthesis and use in determining the sequence of an oligopeptide dimer ligand that optimally binds to a receptor are disclosed. A dimeric oligopeptide mixture set has two oligopeptide portions bonded together by a disulfide bond. Each oligopeptide of a first oligopeptide portion has the same number of 3 to about 10 residues including an oxidized mercaptan-containing residue that forms part of the disulfide bond and an amino acid residue sequence that includes at least one of at least six residues in addition to the oxidized mercaptan-containing residue at the same one or more predetermined positions of the oligopeptide chain. The second portion has an oligopeptide chain having a length of 4 to about 10 residues, including an oxidized mercaptan-containing residue that forms part of the disulfide bond.

Abstract: Disclosed is a method for enhancing an immune response against an antigen by topical administration of an antigen or a portion thereof in conjunction with an enhancer of skin penetration and an inducer of Langerhans cell migration.

Abstract: Linear substituted oligoalkyleneimine molecules and libraries of molecules are disclosed, as are their methods of synthesis and use in acceptor binding assays. Each molecule or chain of a library contains the same number of 2 to about 10 substituted alkyleneimine repeating units, whose substituents are reduced amino acid side chains bonded to the repeating units at a position alpha to the nitrogen atom, and the member chains of a library are present in equimolar amounts. The chains of a library contain one or more predetermined reduced amino acid side chain-substituted repeating units at one or more predetermined positions of the substituted oligoalkyleneimine chain. The library contains equimolar amounts of at least six different reduced amino acid side chain-substituted repeating units at one or more of the same predetermined positions of the substituted oligoalkyleneimine chain. Particularly preferred linear substituted oligoalkyleneimine molecules and libraries are linear substituted oligoethyleneimines.

Abstract: The present invention provides novel opioid peptides. Disclosed are opioid peptides having the general structures Ac-Phe-Arg-Trp-Trp-Tyr-Xaa-NH.sub.2 (SEQ ID NO. 1); Ac-Arg-Trp-Ile-Gly-Trp-Xaa-NH.sub.2 (SEQ ID NO. 2); Trp-Trp-Pro-Lys-His-Xaa-NH.sub.2 (SEQ ID NO. 3); and shorter versions of the latter, namely, Trp-Trp-Pro-Xaa-NH.sub.2 (SEQ ID NO. 4); Tyr-Pro-Phe-Gly-Phe-Xaa-NH.sub.2 (SEQ ID NO. 5); (D)Ile-(D)Met-(D)Ser-(D)Trp-(D)Trp-Gly.sub.n -Xaa-NH.sub.2 (SEQ ID NO. 6); and (D)Ile-(D)Met-(D)Thr-(D)Trp-Gly-Xaa-NH.sub.2 (SEQ ID NO. 7). Within each genus, Xaa is substituted by a specific amino acid. The invention also relates to an opioid peptide having the general structure Tyr-A1-B2-C3-NH.sub.2 (SEQ ID NO. 214), wherein A is D-Nve or D-Nle, B is Gly, Phe, or Trp, and C is Trp or Nap. Also included within the invention are opioid peptides of the general structure Me.sub.x H.sub.y N-Tyr-Tyr-Phe.sub.m -Pro.sub.n -NH.sub.2 (SEQ ID NO.

Abstract: The present invention relates to novel family of peptides which inhibit calmodulin and which have the general structure Ac-A1-B2-C3-D4-E5-F6-NH.sub.2, (SEQ ID No. 1), wherein A1 is (D)Leu or Leu, B2 is (D)Gln, Gln, (D)Trp, or Trp, C3 is (D)Arg, Arg, (D)Ile, or Ile, D4 is (D)Ile, Ile, (D)His, or His, E5 is (D)Leu, Leu, (D)His, or His, and F6 is (D)Trp, Trp, (D)Arg, or Arg. The novel peptides can be used to inhibit the activity of calmodulin. In addition, the present invention relates to pharmaceutical compositions comprising a pharmaceutically acceptable carrier and a calmodulin-inhibitor peptide. These compositions can be used to treat calmodulin related disorders.

Abstract: Sets and libraries of sets of polypeptides that are related in sequence to melittin are disclosed that have antimicrobial, hemolytic and hydrolytically catalytic activities, as are processes for making and using the same. A contemplated set is a mixture of equimolar amounts of a polypeptide of SEQ ID NO:2, and more preferably SEQ ID NO:3.

Abstract: Linear C.sub.1 -C.sub.7 -alkyl peralkylated oligopeptide sets of molecules are disclosed, as are their methods of synthesis and use in acceptor binding assays. Each molecule or chain of a set contains the same number of two to about ten substituted C.sub.1 -C.sub.7 -alkyl peralkylated amino acid residues, and the member chains of a set are present in equimolar amounts. The chains of a set contain one or more predetermined peralkylated amino acid residues at one or more predetermined positions of the peralkylated oligopeptide chain. The set contains equimolar amounts of at least six different peralkylated amino acid residues at one or more of the same predetermined positions of the peralkylated oligopeptide chain. Libraries of such sets, processes for their use and solid support-linked peralkylated sets are also contemplated, as are specific permethylated oligopeptides.

Abstract: Sets and libraries of sets of polypeptides that are related in sequence to melittin are disclosed that have antimicrobial, hemolytic and hydrolyrically catalytic activities, as are processes for making and using the same. A contemplated set is a mixture of equimolar amounts of a polypeptide of SEQ ID NO:2, and more preferably SEQ ID NO:3.

Abstract: The present invention provides novel opioid peptides. Disclosed are opioid peptides having the general structures Ac-Phe-Arg-Trp-Trp-Tyr-Xaa--NH.sub.2 (SEQ ID NO. 1); Ac-Arg-Trp-Ile-Gly-Trp-Xaa--NH.sub.2 (SEQ ID NO. 2); Trp-Trp-Pro-Lys-His-Xaa--NH.sub.2 (SEQ ID NO. 3); and shorter versions of the latter, namely, Trp-Trp-Pro-Xaa--NH.sub.2 (SEQ ID NO. 4); Tyr-Pro-Phe-Gly-Phe-Xaa--NH.sub.2 (SEQ ID NO. 5); (D)Ile-(D)Met-(D)Ser-(D)Trp-(D)Trp-Gly.sub.n -Xaa--NH.sub.2 (SEQ ID NO. 6); and (D)Ile-(D)Met-(D)Thr-(D)Trp-Gly-Xaa--NH.sub.2 (SEQ ID NO. 7). Within each genus, Xaa is substituted by a specific amino acid. The invention also relates to an opioid peptide having the general structure Tyr-A1-B2-C3--NH.sub.2 (SEQ ID NO. 214), wherein A is D-Nve or D-Nle, B is Gly, Phe, or Trp, and C is Trp or Nap. Also included within the invention are opioid peptides of the general structure Pm and red {Me.sub.x H.sub.y N-Tyr-(NMe).sub.z -Tyr-Xaa.sub.z --NH.sub.2 } (SEQ ID NO.

Abstract: The present invention relates to novel family of peptides which inhibit calmodulin and which have the general structure Ac-(D)Leu-A1-B2-C3-D4-E5-NH.sub.2, wherein A1 is (D)Gln or (D)Trp, B2 is (D)Arg or (D)Ile, C3 is (D)Ile or (D)His, D4 is (D)Leu or (D)His and E5 is (D)Trp or (D)Arg. The novel peptides can be used to inhibit the activity of calmodulin. In addition, the present invention relates to pharmaceutical compositions comprising a pharmaceutically acceptable carrier and a calmodulin-inhibitor peptide. These compositions can be used to treat calmodulin related disorders.

Abstract: The present invention provides novel opioid peptides which are selective for the kappa opiate receptor. In one embodiment, the kappa-selective opioid peptides have the general structure Ac-A1-B2-C3-Arg-Tyr-Arg-Tyr-Arg-Arg-Arg-NH.sub.2, (SEQ ID NO. 28), wherein A1 is Tyr or Arg, B2 is Arg or Phe, and C3 is Thr, Phe, or Met. In yet other embodiments, the kappa-selective opioid peptides have the general structure (D)Phe-D4-E5-F6 (SEQ ID NO. 29) or (D)Nle-D4-E5-F6 (SEQ ID NO. 30), where in both of these formulae D4 is (D)NapAla or (D)Phe, E5 is (D)Nle, Trp, or (D)Ile, and F6 is (D)Arg or (D)ChAla.

Abstract: Polypeptides, sets and libraries of sets of polypeptides that are related in sequence to the polypeptide of SEQ ID NO:1 are disclosed that have antimicrobial, hemolytic and hydrolytically catalytic activities, as are processes for making and using the same. A contemplated set is a mixture of equimolar amounts of a polypeptide of SEQ ID NO:2. Particularly preferred polypeptides include those of SEQ ID NOs:3-9.

Abstract: A process for the synthesis of a complex mixture pool of solid support-coupled monomeric repeating unit compounds such as amino acid derivatives is disclosed in which the mixture pool contains an equimolar representation of reacted monomeric repeating unit compounds coupled. Also disclosed is a process for the stepwise synthesis of a complex mixture of coupled or free, unsupported oligomers such as oligopeptides. A set of self-solubilizing, unsupported mixed oligopeptides having one or more predetermined amino acid residues at one or more of the same, predetermined positions in the oligopeptide chain in which the set contains equimolar amounts of a plurality of different amino acid residues, preferably at least six different residues, at one or more of the same predetermined positions of the oligopeptide chain is also disclosed, as are methods of making and using the same.

Abstract: Peptides having Anti-microbial activity and having the formula (KFmoc)ZZZ-NH.sub.2, wherein Z is an amino acid are disclosed. Also disclosed are peptides having anti-trypsin activity and having the formula Ac-rypwz-NH.sub.2, wherein z is a D-amino acid. Also disclosed are compositions containing these peptides and methods of using them.