36 results about "Leucine/Phenylalanine" patented technology

Compounds that modulate natural β amyloid peptide aggregation are provided. The modulators of the invention comprise a peptide, preferably based on a β amyloid peptide, that is comprised entirely of D-amino acids. Preferably, the peptide comprises 3-5 D-amino acid residues and includes at least two D-amino acid residues independently selected from the group consisting of D-leucine, D-phenylalanine and D-valine. In a particularly preferred embodiment, the peptide is a retro-inverso isomer of a β amyloid peptide, preferably a retro-inverso isomer of Aβ17-21. In certain embodiments, the peptide is modified at the amino-terminus, the carboxy-terminus, or both. Preferred amino-terminal modifying groups alkyl groups. Preferred carboxy-terminal modifying groups include an amide group, an acetate group, an alkyl amide group, an aryl amide group or a hydroxy group. Pharmaceutical compositions comprising the compounds of the invention, and diagnostic and treatment methods for amyloidogenic diseases using the compounds of the invention, are also disclosed.

The invention discloses a method for labeling escherichia coli proteome by using SILAC (Stable Isotope Labeling with Amino Acids in Cell Cultures) and a special culture medium. The invention provides a special culture medium for the SILAC-labeled escherichia coli. The special culture medium comprises inorganic salt, histidine hydrochloride, isoleucine, valine, leucine, phenylalanine, tryptophan, serine, heavy stable isotope labeled lysine, arginine, threonine, tyrosine, methionine, adenine sulfate, uracil, vitamin B1 and glucose; and the inorganic salt is Na2HPO4.12H2O, KH2PO4, NaCl, MgSO4, NH4Cl and CaCl2. Experiments prove that, the special culture medium for the SILAC-labeled escherichia coli, disclosed by the invention, creates a condition for researches of labeling the escherichia coli proteome, preparing a quantitative internal label and highly-precisely quantifying the escherichia coli proteome.

The invention relates to the technical field of food processing, in particular to a microbial fermentation source flavor supplement and a preparation method and application thereof. The flavor supplement provided by the invention is formed by mixing the fermentation product of Staphylococcus and Lactobacillus plantarum, and the fermentation medium of Staphylococcus includes valine, leucine, isoleucine and phenylalanine. During application, the meat product is cured by using the marinating liquid containing the flavor supplement, and the prepared bacon product has the unique rich bacon flavor of the bacon made by the traditional process. The method of the invention has a simple process, is suitable for industrial production, can greatly improve the problem of poor flavor of the bacon products produced by the roasting and dehydration process, and has a good market prospect.

The invention discloses a special culture medium for labeling Mycobacterium smegmatis protein by using SILAC. The medium for SILAC labeling provided by the present invention is composed of inorganic salts, histidine hydrochloride, isoleucine, valine, leucine, phenylalanine, tryptophan, serine, heavy stability Isotope-labeled lysine, heavy stable isotope-labeled arginine, threonine, tyrosine, methionine, adenine sulfate, uracil and glucose; the inorganic salts are ammonium sulfate, sodium citrate, hydrogen phosphate Disodium, potassium dihydrogen phosphate, ferric ammonium citrate, magnesium sulfate, calcium chloride, zinc sulfate, and copper sulfate. Experiments have proved that the medium developed by the present invention for labeling Mycobacterium smegmatis SILAC can efficiently label Mycobacterium smegmatis protein within 10 generations, which is for the preparation of quantitative internal standard and the efficient and accurate quantitative proteome comparison. Research creates the conditions.

The present invention provides provides a bacterium of the genus Corynebacterium, in particular of the species Corynebacterium glutamicum, having the ability to excrete an L-amino acid selected from proteinogenic L-amino acids and L-ornithine and new measures for the fermentative production of proteinogenic L-amino acids and L-ornithine by such bacteria.