Classifications

• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
  • A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
  • A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
  • A61K38/00—Medicinal preparations containing peptides
  • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
  • A61K38/55—Protease inhibitors
  • A61K38/56—Protease inhibitors from plants
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
  • A61P3/00—Drugs for disorders of the metabolism
  • A61P3/04—Anorexiants; Antiobesity agents
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
  • A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00

Definitions

• This invention relates to weight reduction by taking with meals a formula in accordance with the invention.
• Chained carbohydrates are degraded to monosaccharides, proteins are degraded to peptides and amino acids, and fats are degraded to free fatty acids and cholesterol.
• nutrients are used by the body as structural components of tissues, cells, enzymes, antibodies, etc.
• proteins are composed of 20 L-amino acids. Eleven of these amino acids can be synthesised by the human body (nonessential amino acids), whereas nine amino acids are such that the body cannot produce (essential amino acids). The latter must therefore be obtained from the diet.
• the adult daily protein requirement is about 60 g, with essential amino acids accounting for about 9 g of this amount.
• appetite suppressants e.g. amfepramone, fenfluramine and sibutramine
• side effects such as insomnia, blood pressure elevation and, in the case of the two first-mentioned drugs, also drug dependence.
• Fenfluramine furthermore, has caused heart valve disease, leading to its withdrawal from the market in most countries.
• Orlistat too, has specific side effects which limit its usefulness.
• the present invention provides a remedy to the unsatisfactory state of affairs described above.
• the hepaticopancreatic duct which empties into the duodenum somewhat distally from the pylorus, starts to discharge trypsinogen, an inactive proenzyme secreted by the pancreas.
• the wall of the duodenum contains an enzyme called enterokinase. Enterokinase converts the inactive trypsinogen to active trypsin which in turn breaks down the chyme-contained proteins into peptides. Trypsin further activates other enzymes responsible for the digestion of food proteins. Trypsin also activates any remaining trypsinogen through an autocatalytic mechanism.
• the 50 - 100 mg of trypsin secreted in conjunction with eating is able to break down into peptides all of the 30-60 g of protein contained in a normal meal. Without the action of trypsin, this digestion of protein will not take place.
• pancreatic diseases sometimes progressing to complete cessation of trypsin secretion.
• enzyme preparation e.g. Pancreatin®. Twin Laboratories Inc., Hauppauge, NY, USA
• digests food proteins thus makes up for the lacking trypsin secretion.
• trypsin inhibitors most of which are proteins by nature. In the presence of trypsin, these compounds bind to trypsin, forming inactive complexes.
• Well known trypsin inhibitors include alpha 1 -antitrypsin, trypstatin, alpha 2-macroglobulin, soybean trypsin inhibitors, egg-white trypsin inhibitors and aprotinin. Each of these is available commercially, and the latter substance is also registered as a medicinal product (e.g. Trasylol®. Bayer AG, Leverkusen, Germany).
• Therapeutic oral administration of trypsin inhibitors and trypsin inactivation in the alimentary tract have been published for instance in patent documents JP 2-250823 (A) and US 5607671.
• the present invention is aimed at preventing the absorption of proteins. This is achieved by oral administration of one, of the above-mentioned trypsin inhibitors with meals whereby the trypsin inhibitor moves along the alimentary tract to trypsin's site of action in the intestine.
• soybean trypsin inhibitor Type ll-S. Sigma Chemical Co., St. Louis, MO, USA
• one weight unit of the inhibitor can inactivate 2.5 weight units of trypsin secreted into the duodenum by the pancreas.
• the proteins contained in the food are not digested and cannot be absorbed. This results in artificial protein malabsorption which inevitably leads to loss of body weight.
• the present invention includes oral coadministration of required amounts of all essential amino acids in free form, together with the trypsin inhibitor.
• the essential amino acids are L- phenylalanine, L-histidine, L-isoleucine, L-leucine, L-lysine, L-methionine, L- threonine, L-tryptophan and L-valine. While weight is lost, these essential amino acids prevent the development of malabsorption syndrome.
• the nonessential amino acids do not function as required by the invention, they cannot by used as active substances in its embodiments. Free amino acids are fully absorbed from the alimentary tract, and their absorption is not affected by the trypsin inhibitor.
• the present invention allows the amount of absorbed food protein and the energy therein to be reduced without causing a deficiency of essential amino acids.
• the result is weight reduction without disturbance of the nutritional status of the body.
• the trypsin inhibitor is preferably transported to trypsin's site of action in the intestine in a formulation that does not release the active substance until it has passed the stomach. This is achieved by application of a "programmed delivery pattern" in the pharmaceutical formulation.
• enteric coating suitable for embodiments of the invention include polyvinyl acetate (Colorcon®. Colorcon Inc., West Point, PA, USA) and the acrylic acid derivatives described in patent document JP 2-250823 (A).
• Said enteric coatings dissolve when the ambient pH exceeds 4.7. As such pH is characteristic of the intestine right from the beginning of the duodenum, release of the active substance is accomplished exactly in this desired location below the stomach. It then mixes with trypsin in the chyme, causing inhibition of trypsin activity.
• the person concerned is not required to subdue, limit or regulate his/her hunger or appetite in any way.
• One dose of a preparation in accordance with the invention is as follows:
• Said dose (2 g) may be formulated, for instance, as a sachet or capsule containing a single-dose of powder or as a tablet containing the powder in combination with approved excipients or, for instance, an aqueous solution of approved excipients and the active ingredients.
• any nontoxic compound that inactivates trypsin can be used for trypsin inhibition.
• Proteinous trypsin inhibitors can be enteric encapsulated, for instance, by coating microgranules with polyvinyl acetate (Colorcon®). Such granules can be administered either on their own or, for instance, in a gelatine capsule together with essential amino acids, or the two entities can be taken as separate preparations, albeit during the same meal.

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• Health & Medical Sciences (AREA)
• Life Sciences & Earth Sciences (AREA)
• Chemical & Material Sciences (AREA)
• Medicinal Chemistry (AREA)
• Pharmacology & Pharmacy (AREA)
• Animal Behavior & Ethology (AREA)
• General Health & Medical Sciences (AREA)
• Public Health (AREA)
• Veterinary Medicine (AREA)
• Engineering & Computer Science (AREA)
• Epidemiology (AREA)
• Bioinformatics & Cheminformatics (AREA)
• Chemical Kinetics & Catalysis (AREA)
• Gastroenterology & Hepatology (AREA)
• Immunology (AREA)
• Proteomics, Peptides & Aminoacids (AREA)
• Botany (AREA)
• General Chemical & Material Sciences (AREA)
• Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
• Organic Chemistry (AREA)
• Obesity (AREA)
• Diabetes (AREA)
• Hematology (AREA)
• Child & Adolescent Psychology (AREA)
• Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
• Medicines Containing Plant Substances (AREA)
• Coloring Foods And Improving Nutritive Qualities (AREA)
• Medicines Containing Material From Animals Or Micro-Organisms (AREA)
• Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
• Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
• Medicinal Preparation (AREA)
• Saccharide Compounds (AREA)
• Diaphragms For Electromechanical Transducers (AREA)

Priority Applications (6)

Applications Claiming Priority (2)

Publications (1)

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Family Applications (1)

Country Status (11)

Cited By (2)

Citations (9)

• 2002
  • 2002-02-20 FI FI20020332A patent/FI109970B/fi active
• 2003
  • 2003-02-12 CA CA002476771A patent/CA2476771A1/en not_active Abandoned
  • 2003-02-12 DE DE60323062T patent/DE60323062D1/de not_active Expired - Fee Related
  • 2003-02-12 WO PCT/FI2003/000107 patent/WO2003070276A1/en not_active Ceased
  • 2003-02-12 ES ES03702672T patent/ES2314175T3/es not_active Expired - Lifetime
  • 2003-02-12 AU AU2003205795A patent/AU2003205795A1/en not_active Abandoned
  • 2003-02-12 AT AT03702672T patent/ATE405290T1/de not_active IP Right Cessation
  • 2003-02-12 EP EP03702672A patent/EP1482976B1/en not_active Expired - Lifetime
  • 2003-02-12 CN CNA038043793A patent/CN1729017A/zh active Pending
  • 2003-02-12 JP JP2003569231A patent/JP2005523284A/ja active Pending
  • 2003-02-12 US US10/504,148 patent/US20050096266A1/en not_active Abandoned

Patent Citations (9)

Non-Patent Citations (3)

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