56 results about "Depsipeptide" patented technology

The present invention provides a therapeutic agent of kidney cancer, which comprises FK228 of the formula (I) or a salt thereof. FK228 or a salt thereof, which is an active ingredient in the present invention, shows a superior antitumor activity in vivo against kidney cancer.

The present invention relates to novel depsipeptide compounds. The invention also relates to pharmaceutical compositions of these compounds and methods of using these compounds as antibacterial compounds. The invention also relates to methods of producing these novel depsipeptide compounds and intermediates used in producing these compounds.

The invention relates to a method or process for the chemical manufacture of depsipeptides of the formula I employing an aldehyde acetal intermediate,

wherein the symbols have the meaning defined in the description, to new intermediates and their manufacture, as well as related invention embodiments.

The invention discloses a new method for preparing depsipeptide FK228, comprising the following steps of: firstly forming annular polypeptide in a ring-closing way through the condensation reaction of an amido bond; and then forming the coupling of sulfide-sulfide bonds through radical reaction catalyzed by iodine by using a mixed solution of methylene dichloride and methanol as a solvent so as to synthesize the FK228. The preparation method of the FK228 has the advantages of easy operation and low cost, primarily discloses a process for preparing gram-grade FK228, greatly enhances the yield compared with past literatures and patents and provides new selection for the preparation and the production of the FK228.

The invention relates to a microbe-derived pesticide, and concretely relates to a depsipeptide compound, and a preparation method and an application thereof. The depsipeptide compound is represented by formula (1). The depsipeptide compound is obtained by through fermenting culture of Beauveria felina AS-70 (preserved in China General Microbiological Culture Collection Center on Sep. 29, 2012 with the preservation number of CGMCC NO.6643), and through extraction and separation. A result of identification of the chemical structure of the compound through nuclear magnetic resonance and mass spectrum shows that the compound has good insecticidal activity.

The present invention relates to pyrrolidine compounds of the general structure:

where n is an integer 1-6 and R is hydrogen or a C₁ to C₆ straight chain or branched alkyl group, and wherein when n=1, R=CH₃ or H, useful for re-sensitizing vancomycin resistant Gram-positive bacteria in which resistance results from the conversion of an amide bond to an ester bond on the cell wall peptide precursors of the bacteria.

A Compound of structure (IX) or (X) or a pharmaceutically acceptable salt thereof, wherein: X is —C(═O)N(R₁₀)— or —CH(OPr₃)—; R₇, R₉ and R₁₀ are the same or different and represent hydrogen or an amino acid side chain moiety from either a natural or an unnatural amino acid; Pr₁ and Pr₂ are the same or different and represent hydrogen or a thiol protecting group; Pr₃ is hydrogen or an alcohol protecting group; R₁, R₂, R₅ and R₆ are the same or different and represent hydrogen or an amino acid side chain moiety from either a natural or an unnatural amino acid, or R₁ and R₂ and/or R₅ and R₆, taken together with the carbon atom to which they are attached, form a spirocyclic moiety, with the proviso that: each of R₁ and R₂ is not hydrogen, or each of R₅ and R₆ is not hydrogen.

The invention relates to a method or process for the chemical manufacture of depsipeptides of the formula I,

wherein the symbols have the meaning defined in the description, to new intermediates and their manufacture, as well as related invention embodiments.

Crystals of a depsipeptide derivative of formula (IV):having an antiparasitic activity and methods for producing such crystals. Such crystals include crystals (I), (II) and (III) that have particular physicochemical properties or characteristics, such as excellent filtration properties during crystallization, great fluidity, good specific volume. As a consequence, such crystals have improved handling ability during production resulting in enhanced production efficiency and increased crystal yield. Methods are also provided for producing such crystals.

The present invention relates to a method of forming a peptide of Formula (I) (P¹-Xaa¹-Xaa²-P²) by ligating a first peptide of Formula (II) (P¹-Xaa¹-X—R, wherein X is O or S) to a second peptide of Formula (II I) (Xaa¹-Xaa²-P²) by enzymatically cleaving the bond between “Asx” and “X” in the first peptide of Formula (II) and ligating the fragment P¹-Asx of the first peptide to the second peptide of Formula (III), wherein the enzymatic cleavage and ligation reaction is catalyzed by butelase 1 (SEQ ID NO: 1) and the peptide of Formula (I) is a depsipeptide, preferably a thiodepsipeptide. Further encompassed are peptides and dendrimeric peptide assemblies prepared using the presently disclosed method, as well as use of the dendrimeric peptide assemblies as a vaccine, medicament, or diagnostic agent, particularly as an antimicrobial agent.

The invention discloses a liraglutide synthesis method, which comprises the following steps: 1, preparing a Fmoc-Gly-Wang resin; 2, preparing a fully-protected peptide resin from the Fmoc-Gly-Wang resin, protected amino acid and Pal-Glu, the fully-protected peptide resin comprising Depsipeptide Units; 3, performing TFA pyrolysis on the peptide resin to obtain crude peptide; 4, dissolving the crudepeptide obtained in Step 3, regulating the PH and performing ester bond to amido bond reaction to obtain a liraglutide crude product. According to the method, the Depsipeptide Units are introduced toobtain the fully-protected peptide resin and then pyrolysis and ester bond to amido bond reaction are performed to obtain a target product; by introduction of the Depsipeptide Units, problems about synthesis of difficult sequences of the liraglutide can be solved, and the purity and the yield of the synthesized crude peptide can be greatly improved.