Abstract: The invention provides a broad spectrum antimicrobial compound that includes a tryptophan-rich peptide exhibiting antimicrobial activity. A method of microbicidal inhibition or microbistatic inhibition of microbial growth is also provided. The method includes administering to an environment capable of sustaining microbial growth a microbicidally or microbistatically effective amount of a tryptophan-rich peptide exhibiting antimicrobial activity.

Abstract: This invention relates to a diapause hormone, a novel polypeptide, comprising 24 amino acids residues designated by the following amino acid sequence: ##STR1## wherein X is Cys (SEQ ID NO:1) or Trp (SEQ ID NO:2) and R is OH or NH.sub.2.

Abstract: This invention provides a method of prophylactically preventing the onset, preventing the development, and arresting the progression of insulin dependent diabetes mellitus in a mammal by administering an effective amount of rapamycin either alone or in combination with insulin.

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: A compound of formula (I): ##STR1## in which: R.sub.1 and R.sub.2, which are identical or different, represent hydrogen, or alkyl, cycloalkyl or benzyl,B represents a residue of an aromatic amino acid,A represents a peptide residue comprising from one to three amino acids, in cyclic or linear form, and medicaments containing the same, are disclosed.

Abstract: Peptides are provided which are suitable for the treatment of pain and gastro-intestinal disorders, such as diarrhea, and are represented by the structure: ##STR1## where values for the substituents and n are disclosed herein. Methods for preparing these peptides by solution and solid phase syntheses are also provided. Pharmaceutical compositions utilizing these peptides in a pharmaceutically effective amount and methods of treatment using them are provided.

Abstract: Disclosed are a peptide derivative represented by the formula [I] or a pharmaceutically acceptable salt thereof: ##STR1## wherein A, B, C, D, E and F each represent amino acid residues, and satisfy any one condition of (i) A=Ser, B=Ser, C=Ser, D=Leu, E=Met and F=Phe, (ii) A=Ser, B=Ser, C=Ser, D=Trp, E=Leu and F=Phe, and (iii) A=Thr, B=Phe, C=Thr, D=Tyr, E=Lys and F=Tyr; and W, X, Y and Z each represent amino acid residues, and satisfy any one condition of (i) at least one of W and Y is an amino acid residue other than an L-alanine residue or other than an L-cysteine residue, (ii) X is an amino acid residue other than an L-Lysine residue, and (iii) Z is an amino acid residue other than an L-aspartic acid residue; (2) a method for producing the peptide derivative or the salt thereof; and (3) an agent for improving a circulatory function mainly comprising the peptide derivative or the salt thereof, such as a vasodilator or a vasoconstrictor.

Abstract: Administration of a Corticotropin-Releasing Factor (or a salt or analog thereof) decreases the leakage of blood components into brain tissue produced by various adverse medical conditions and reduces bleeding when muscle tissues are cut and handled, such as in plastic and reconstructive surgery. A method of treating a patient for injury to or disease of the brain, central nervous system, or musculature in which edema is a factor comprises administering to the patient a Corticotropin-Releasing Factor (or a salt or analog) in an amount effective to decrease vascular permeability in the injured or diseased brain, nervous system tissue or musculature, and thereby to reduce edema. Administration in accordance with the method can be about two hours before surgery, or can be up to three days after injury.

Abstract: Secretory leader sequences, for use in secreting heterologous polypeptides in yeast, are formed by fusing part of the human serum albumin pre-sequence or part of the Kluyveromyces lactis killer toxin pre-sequence to the Saccharomyces cerevisiae mating factor alpha-1 KEX2 cleavage recognition site. The resulting fusion leader sequences are:(a) H.sub.2 N-Met-Lys-Trp-Val-Ser-Phe-Ile-Ser-Leu-Leu-Phe-Leu-Phe-Ser-Ser-Ala-Tyr-Ser- Arg-Ser-Leu-Asp-Lys-Arg-COOH or(b) H.sub.2 N-Met-Asn-Ile-Phe-Tyr-Ile-Phe-Leu-Phe-Leu-Leu-Ser-Phe-Val-Gln-Gly-Ser-Leu- Asp-Lys-Arg-COOHConservative variations are also encompassed.

Abstract: This invention discloses that certain fragments of a pulmonary surfactant protein exhibit unexpected surface activity. These protein fragments are useful in preparing formulations for the treatment of respiratory disease.

Abstract: The present invention relates to novel "pseudo" nonapeptide and decapeptide derivatives of LHRH. More particularly the present invention relates to derivatives of LHRH wherein the nitrogen atom of at least one of the amide bonds has been alkylated.

Abstract: An onco-developmentally regulated .alpha.-N-acetylgalactosaminyltransferase isolated as a component of a particulate membrane fraction separated from cell and tissue homogenates and having the following characteristics:(a) Activity in Various Cells and Tissues--present in human fetal lung fibroblasts, hepatoma tissues and placenta, but absent from normal adult liver, lung, kidney and spleen tissues;(b) Substrate Specificity--acts on polypeptides comprising a sequence val-thr-his-pro-gly-tyr by catalyzing u-N-acetylgalactosaminylation at the thr residue of the sequence;(c) Requirements for Metal Ion--requires metal ion for activity in 25 mM tris buffer, pH 7.6;(d) Optimal pH--optimal pH is about 7.6 assayed in hepatoma cell homogenate in tris buffer and at a pH of about 6 to about 7 assayed in hepatoma cell homogenate enzyme activity is higher in 2(N-morpholino)ethanesulfonic acid than in cacodylate buffer; and(e) Km--apparent Km for UDP - GalNAc is about 48 .mu.M.

Abstract: Ipoxantine derivatives of general formula (I): ##STR1## both as racemate and chiral forms and the salts thereof with pharmacologically acceptable cations, wherein n is an integer comprised between 2 and 6, and A is the residue of a dipeptide, tripeptide, tetrapeptide and pentapeptide selected, respectively, from the groups consisting of:(a) glycyl-aspartate, alanyl-glycine, glycyl-glycine, aspartyl-arginine, leucyl-arginine;(b) arginyl-lysyl-aspartate, aspartyl-lysyl-arginine, lysyl-prolyl-arginine, prolyl-prolyl-arginine, lysyl-histidyl-glycinamide, prolyl-phenilalanyl-arginine, phenylalanyl-prolyl-arginine;(c) arginyl-lysyl-aspartyl-valine (SEQ ID NO: 1), valyl-aspartyl-lysyl-arginine (SEQ ID NO: 2), threonylvalyl-leucyl-histidyne (SEQ ID NO: 3); and(d) arginyl-lysyl-aspartyl-valyl-tyrosine (SEQ ID NO: 4);are endowed with immunomodulating activity and can be formulated in orally or parenterally administrable pharmaceutical compositions.

Abstract: Tetrapeptides and pentapeptides are disclosed which are capable of regulating the function of cells of the mammalian immune system. Also provided are pharmaceutical compositions containing the peptides and methods of use thereof.

Abstract: A process for inhibiting growth of a target cell comprising administering to a host or to a target cell or virus a biologically active peptide which includes one of the following basic structures; R.sub.1 -R.sub.1 -R.sub.2 -R.sub.1 -R.sub.1 -R.sub.2 -R.sub.2 -R.sub.1 -R.sub.1 -R.sub.2 -R.sub.2 -R.sub.1 -R.sub.2 -R.sub.2 ; R.sub.2 -R.sub.1 -R.sub.1 -R.sub.2 -R.sub.2 -R.sub.1 -R.sub.2 -R.sub.2 -R.sub.1 -R.sub.1 -R.sub.2 -R.sub.2 -R.sub.1 -R.sub.1 ; or R.sub.1 -R.sub.2 -R.sub.1 -R.sub.1 -R.sub.2 -R.sub.2 -R.sub.1 -R.sub.1 -R.sub.2 -R.sub.2 -R.sub.1 -R.sub.2 -R.sub.2 -R.sub.1 -R.sub.1 -R.sub.2 -R.sub.2 -R.sub.1, wherein R.sub.1 is a hydrophobic amino acid, and R.sub.2 is a basic hydrophilic or neutral hydrophilic amino acid. A preferred peptide is of the structural formula:(SEQ ID NO:3).Substitution and deletion analogues of this peptide can be prepared that have increased biological activity. Such peptides can be employed as pharmaceuticals.

Abstract: A medicament for prevention and remedy of diseases of pancreas and others is disclosed, which is characterized by containing as an effective ingredient thereof a nonapeptide having the following amino acid configuration:pGlu-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asnor an ester and amide at the carboxyl group of the C-terminal of the asparagine or a pharmacologically acceptable salt thereof.

Abstract: Peptides corresponding to epitopes of HTLV-2 proteins are provided. These peptides are immunologically reactive with HTLV-2 specific antibodies. Several of the peptides are sufficiently unreactive to antibodies to HTLV-1 to distinguish between antibodies which recognize HTLV-1 and those which recognize HTLV-2. Thus HTLV-1 infections can be distinguished from HTLV-2 infections. The peptides are useful in assays for detection of HTLV-2 infection or exposure. The peptides are also useful as vaccine compositions against HTLV-2. Antibodies generated in response to immunization by the peptides are also provided.

Abstract: A process for producing an optically active .alpha.-substituted organic acid represented by formula (II), comprising the steps of (a) treating a racemic substituted nitrile or amide represented by formula (I) with a microorganism selected from the group consisting of the microorganisms of genuses Alcaligenes, Pseudomonas, Rhodopseudomonas, Corynebacterium, Acinetobacter, Bacillus, Mycobacterium, Rhodococcus and Candida, or preparations thereof; and (b) recovering the resulting optically active u-substituted organic acid represented by formula (II): ##STR1## wherein R.sub.1 and R.sub.2 each represent a halogen atom, a hydroxyl group, a substituted or unsubstituted alkyl group, a substituted or unsubstituted cycloalkyl group, a substituted or unsubstituted alkoxy group, a substituted or unsubstituted aryl group, a substituted or unsubstituted aryloxy group or a substituted or unsubstituted heterocyclic group with the proviso that R.sub.1 and R.sub.

Abstract: Membrane anchoring peptides which are part of the heavy chain of an associated immunoglobulin (IgM, IgD, IgA, IgE, or IgG), span the cell membrane lipid bilayer of B cells thereby affixing the associated immunoglobulin to the cell membrane surface. The extracellular segments of these peptides are unique for different isotypes, but tend to be very similar among different subclasses of a particular isotype. The extracellular segments form in whole or in part an epitope unique to the B cells which produce each isotype. These membrane-bound immunoglobulin isotype-specific ("migis") extracellular epitopes are not present on the secreted, soluble form of the immunoglobulins, which are not bound to the cell surface by the membrane anchoring peptides. The antibodies of the invention (and other related products) bind the extracellular migis epitopes.

Abstract: Compounds and methods for blocking the effects of diabetes-associated peptide, or "amylin", a hormone found in the amyloid masses of Type 2 diabetics. This putative hormone has been discovered to function both to inhibit insulin secretion and to inhibit glycogen synthesis. Regulation is accomplished by blocking the binding of amylin or amylin agonists, including calcitonin gene related peptide (CGRP], or biologically active sub-peptides thereof. Inhibitors include substituted peptides or sub-peptides of amylin or CGRP, cross-linked amylin and amylin agonists, synthetic amylin, anti-amylin receptor antibodies and anti-idiotype antibodies, and antibodies directed to amylin and amylin agonist active sites. Other antagonists include organic compounds which can be screened and assayed for anti-amylin effects by disclosed methods.