54results about "Secretins" patented technology

Compositions comprising activatable recombinant neurotoxins and polypeptides derived therefrom. The invention also comprises nucleic acids encoding such polypeptides, and methods of making such polypeptides and nucleic acids.

The invention relates generally to methods for treating acute pancreatitis in patients. The methods comprise administering a therapeutically effective amount of a pharmaceutical composition comprising secretin and a pharmaceutically acceptable carrier.

A therapeutic method for treating an individual diagnosed with PDD pervasive developmental disorder comprises determining the efficacy of digestive enzyme administration for the treatment of the individual based on a measure of the individual's chymotrypsin level, and administering digestive enzymes to the individual based on the determination of the measure of the individual's chymotrypsin level. A method for reducing the amount of methylphenidate (Ritalin) being taken by an individual with attention deficit disorder (ADD) or attention deficit hyperactivity disorder (ADHD) by administering a therapeutic amount of digestive enzymes is also provided.

A compound is provided that has the formulaNH2CH2CH2CHR1C(O)N—R   (I)where R1 is p-chlorophenyl, R is a moiety capable of crossing the blood brain barrier and is as a free compound serotonin, dopamine blood brain barrier (BBB) peptide, membrane translocating protein, TAT peptides, bradykinin, beta-endorphin, bombesin, calcitonin, cholecystokinin, an enkephalin, dynorphin, insulin, gastrin, substance P, neurotensin, glucagon, secretin, somatostatin, motilin, vasopressin, oxytocin, prolactin, thyrotropin, an angiotensin, galanin, neuropeptide Y, thyrotropin-releasing hormone, gonadotropnin-releasing hormone, growth hormone-releasing hormone, luteinizing hormone, vasoactive intestinal peptide transferrin, glucosylamine, amino saccharin, lactylamine, leucine, tryptophan, glutamate and amino cholines.

A composition is provided having the formulawhere R1 and R2 are each independently H or a C1-C4 hydrocarbon; R3 is H, and R4 is a moiety capable of crossing the blood brain barrier selected from the group consisting of: an amino acid, a peptide, transferrin, gluconate, lactate, citrate, malate, fumarate, benzoate, salicylate, pyruvate and propionate. The composition includes 4-aminopyridine and a transporter species which allows for improved transport of the aminopyridine across the blood brain barrier thereby reducing systemic side effects of aminopyridine administration.

This invention pertains to a sustained release complex of one or more peptides, one or more proteins or a combination thereof immobilized on an absorbable polymer microparticle optionally having an absorbable polymer coating. The microparticle complex of this invention comprises a peptide(s) and / or protein(s) which have at least one amino group and / or at least one carboxyl group per molecule and a solid absorbable polyester microparticle having surface and subsurface carboxylic group or amino groups in sufficient amounts to bind the peptide(s) and / or protein(s) so that the immobilized peptide(s) or protein(s) represent 0.1% to 30% of the total mass of the microparticle complex. The microparticle complex with immobilized peptide(s) and / or protein(s) are optionally further encased individually or in groups with an absorbable polymer to control, further, the release of the immobilized peptide(s) and / or protein(s). To control the release of the immobilized peptide(s) and / or protein(s) even further, the encased microparticles can be incorporated into a composition with an absorbable gel-forming liquid that transforms to a flexible gel or semi-solid upon contacting water in the biologic environment.

The present invention relates to acylated GIP analogs which have dual GIP and GLP-1 activity, and their use in the treatment of metabolic disorders.

Disclosed is a method for refolding a protein or peptide that does not contain essential disulfides and that contains at least one free cysteine residue. Also disclosed are polymer IFN-γ conjugates that have been created by the chemical coupling of polymers such as polyethylene glycol moieties to IFN-γ, particularly via a free cysteine in the protein. Also disclosed are analogs of bioactive peptides that may be used to create longer acting versions of the peptides, including analogs of glucagon, glucagon-like peptide-1 (GLP-1), GLP-2, Gastric inhibitory peptide (GIP), PYY, exendin, ghrelin, gastrin, amylin, and oxyntomodulin.

Disclosed is a method for refolding a protein or peptide that does not contain essential disulfides and that contains at least one free cysteine residue. Also disclosed are polymer IFN-γ conjugates that have been created by the chemical coupling of polymers such as polyethylene glycol moieties to IFN-γ, particularly via a free cysteine in the protein. Also disclosed are analogs of bioactive peptides that may be used to create longer acting versions of the peptides, including analogs of glucagon, glucagon-like peptide-1 (GLP-1), GLP-2, Gastric inhibitory peptide (GIP), PYY, exendin, ghrelin, gastrin, amylin, and oxyntomodulin.

A method for protecting a peptide from peptidase activity in vivo, the peptide being composed of between 2 and 50 amino acids and having a C-terminus and an N-terminus and a C-terminus amino acid and an N-terminus amino acid is described. In the first step of the method, the peptide is modified by attaching a reactive group to the C-terminus amino acid, to the N-terminus amino acid, or to an amino acid located between the N-terminus and the C-terminus, such that the modified peptide is capable of forming a covalent bond in vivo with a reactive functionality on a blood component. In the next step, a covalent bond is formed between the reactive group and a reactive functionality on a blood component to form a peptide-blood component conjugate, thereby protecting said peptide from peptidase activity. The final step of the method involves the analyzing of the stability of the peptide-blood component conjugate to assess the protection of the peptide from peptidase activity.

Provided are methods of treatment of many different diseases and disorders using micelle and sterically stabilized crystalline compounds of the invention.

The invention relates generally to methods for preventing post endoscopic retrograde cholangiopancreatography pancreatitis (ERCP). The method comprises administering a therapeutically effective amount of a pharmaceutical composition comprising secretin and a pharmaceutically acceptable carrier.

There is provided a novel series of synthetic analogs of hGH-RH(1-29)NH2 (SEQ ID NO: 1) and hGH-RH(1-30)NH2. Of particular interest are those carrying PhAc, N-Me-Aib, Dca, Ac-Ada, Fer, Ac-Amc, Me-NH-Sub, PhAc-Ada, Ac-Ada-D-Phe, Ac-Ada-Phe, Dca-Ada, Dca-Amc, Nac-Ada, Ada-Ada, or CH3—(CH2)10—CO-Ada, at the N-Terminus and β-Ala, Amc, Apa, Ada, AE2A, AE4P, ε-Lys(α-NH2), Agm, Lys(Oct) or Ahx, at the C-terminus. These analogs inhibit the release of growth hormone from the pituitary in mammals as well as inhibit the proliferation of human cancers, and inhibit the hyperplastic and benign proliferative disorders of various organs, through a direct effect on the cancerous and non-malignant cells. The stronger inhibitory potencies of the new analogs, as compared to previously described ones, result from replacement of various amino acids.

The present invention relates to the field of biopharmaceuticals, and in particular to a protein, a protein conjugate, a pharmaceutical composition and its use for treating diabetes. The fusion protein of the present invention is obtained by linking two polypeptides, wherein one polypeptide is an interleukin-1 receptor antagonistic protein or an analogue thereof, and another polypeptide is GLP-1 receptor binding polypeptide or an analogue thereof, or an insulin receptor binding polypeptide or an analogue thereof, or a GIP receptor binding polypeptide or an analogue thereof. The fusion proteins of the present invention and conjugates thereof have a significant efficacy in treating diabetes, and can be used in a lower dose, resulting in marked reduction in side effects.