IL98349A - Diphylase lipopeptide - Google Patents

Diphylase lipopeptide

Info

Publication number: IL98349A
Authority: IL; Israel
Prior art keywords: deacylase; kcl; ala; activity; gly
Prior art date: 1990-06-07

Application number

IL9834991A

Other languages

English (en)

Hebrew (he)

Other versions

IL98349A0 (en

Original Assignee

Lilly Co Eli

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1990-06-07

Filing date

1991-06-03

Publication date

1995-05-26

1991-06-03 Application filed by Lilly Co Eli filed Critical Lilly Co Eli

1992-07-15 Publication of IL98349A0 publication Critical patent/IL98349A0/xx

1995-05-26 Publication of IL98349A publication Critical patent/IL98349A/en

Links

108010028921 Lipopeptides Proteins 0.000 title description 4
FAUOJMHVEYMQQG-HVYQDZECSA-N echinocandin B Chemical compound C1([C@H](O)[C@@H](O)[C@H]2C(=O)N[C@H](C(=O)N3C[C@H](C)[C@H](O)[C@H]3C(=O)N[C@H](O)[C@H](O)C[C@@H](C(N[C@H](C(=O)N3C[C@H](O)C[C@H]3C(=O)N2)[C@@H](C)O)=O)NC(=O)CCCCCCC\C=C/C\C=C/CCCCC)[C@@H](C)O)=CC=C(O)C=C1 FAUOJMHVEYMQQG-HVYQDZECSA-N 0.000 claims abstract description 60
230000000694 effects Effects 0.000 claims abstract description 59
108010062092 echinocandin B Proteins 0.000 claims abstract description 52
238000000034 method Methods 0.000 claims abstract description 28
108010069514 Cyclic Peptides Proteins 0.000 claims abstract description 9
102000001189 Cyclic Peptides Human genes 0.000 claims abstract description 9
230000020176 deacylation Effects 0.000 claims abstract description 7
238000005947 deacylation reaction Methods 0.000 claims abstract description 7
239000000833 heterodimer Substances 0.000 claims abstract description 4
WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 claims description 93
239000001103 potassium chloride Substances 0.000 claims description 47
235000011164 potassium chloride Nutrition 0.000 claims description 47
239000000872 buffer Substances 0.000 claims description 34
229910000402 monopotassium phosphate Inorganic materials 0.000 claims description 25
IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 claims description 16
150000003839 salts Chemical class 0.000 claims description 14
239000000758 substrate Substances 0.000 claims description 12
-1 8-methyldecanoyl Chemical group 0.000 claims description 11
239000003446 ligand Substances 0.000 claims description 9
229910052921 ammonium sulfate Inorganic materials 0.000 claims description 8
239000012736 aqueous medium Substances 0.000 claims description 7
125000002669 linoleoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])/C([H])=C([H])\C([H])([H])/C([H])=C([H])\C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 7
239000000203 mixture Substances 0.000 claims description 6
125000001312 palmitoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 6
150000001413 amino acids Chemical class 0.000 claims description 5
238000004519 manufacturing process Methods 0.000 claims description 4
230000003197 catalytic effect Effects 0.000 claims description 3
238000005341 cation exchange Methods 0.000 claims description 3
150000001875 compounds Chemical class 0.000 claims description 3
125000003074 decanoyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C(*)=O 0.000 claims description 3
238000001914 filtration Methods 0.000 claims description 3
230000002209 hydrophobic effect Effects 0.000 claims description 3
230000003993 interaction Effects 0.000 claims description 3
229910001514 alkali metal chloride Inorganic materials 0.000 claims description 2
229910001963 alkali metal nitrate Inorganic materials 0.000 claims description 2
239000007864 aqueous solution Substances 0.000 claims description 2
238000010438 heat treatment Methods 0.000 claims description 2
229910052739 hydrogen Inorganic materials 0.000 claims description 2
239000001257 hydrogen Substances 0.000 claims description 2
229910017053 inorganic salt Inorganic materials 0.000 claims description 2
238000002156 mixing Methods 0.000 claims description 2
125000001419 myristoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 2
125000004435 hydrogen atom Chemical group [H]* 0.000 claims 1
108090000790 Enzymes Proteins 0.000 abstract description 49
102000004190 Enzymes Human genes 0.000 abstract description 49
241000187840 Actinoplanes utahensis Species 0.000 abstract description 13
238000005277 cation exchange chromatography Methods 0.000 abstract description 9
108010049047 Echinocandins Proteins 0.000 abstract description 8
238000002523 gelfiltration Methods 0.000 abstract description 7
238000004191 hydrophobic interaction chromatography Methods 0.000 abstract description 4
239000002207 metabolite Substances 0.000 abstract description 3
239000002738 chelating agent Substances 0.000 abstract description 2
229910052751 metal Inorganic materials 0.000 abstract description 2
239000002184 metal Substances 0.000 abstract description 2
239000003774 sulfhydryl reagent Substances 0.000 abstract description 2
150000002632 lipids Chemical class 0.000 abstract 1
235000002639 sodium chloride Nutrition 0.000 description 16
102000004169 proteins and genes Human genes 0.000 description 15
108090000623 proteins and genes Proteins 0.000 description 15
238000006243 chemical reaction Methods 0.000 description 12
238000000746 purification Methods 0.000 description 11
229920002684 Sepharose Polymers 0.000 description 9
238000004587 chromatography analysis Methods 0.000 description 9
239000000243 solution Substances 0.000 description 7
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
238000003556 assay Methods 0.000 description 6
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
229940121375 antifungal agent Drugs 0.000 description 4
238000004128 high performance liquid chromatography Methods 0.000 description 4
FGIUAXJPYTZDNR-UHFFFAOYSA-N potassium nitrate Chemical compound [K+].[O-][N+]([O-])=O FGIUAXJPYTZDNR-UHFFFAOYSA-N 0.000 description 4
239000011347 resin Substances 0.000 description 4
229920005989 resin Polymers 0.000 description 4
GUPXYSSGJWIURR-UHFFFAOYSA-N 3-octoxypropane-1,2-diol Chemical compound CCCCCCCCOCC(O)CO GUPXYSSGJWIURR-UHFFFAOYSA-N 0.000 description 3
239000012506 Sephacryl® Substances 0.000 description 3
125000002252 acyl group Chemical group 0.000 description 3
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 3
235000011130 ammonium sulphate Nutrition 0.000 description 3
230000015572 biosynthetic process Effects 0.000 description 3
125000004122 cyclic group Chemical group 0.000 description 3
238000000855 fermentation Methods 0.000 description 3
230000004151 fermentation Effects 0.000 description 3
238000002955 isolation Methods 0.000 description 3
239000002609 medium Substances 0.000 description 3
229910021645 metal ion Inorganic materials 0.000 description 3
239000008188 pellet Substances 0.000 description 3
238000002360 preparation method Methods 0.000 description 3
239000011541 reaction mixture Substances 0.000 description 3
239000011780 sodium chloride Substances 0.000 description 3
VWDWKYIASSYTQR-UHFFFAOYSA-N sodium nitrate Inorganic materials [Na+].[O-][N+]([O-])=O VWDWKYIASSYTQR-UHFFFAOYSA-N 0.000 description 3
238000005063 solubilization Methods 0.000 description 3
230000007928 solubilization Effects 0.000 description 3
239000002904 solvent Substances 0.000 description 3
239000012134 supernatant fraction Substances 0.000 description 3
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 2
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
230000002159 abnormal effect Effects 0.000 description 2
238000004458 analytical method Methods 0.000 description 2
230000000843 anti-fungal effect Effects 0.000 description 2
230000003115 biocidal effect Effects 0.000 description 2
239000003638 chemical reducing agent Substances 0.000 description 2
108010090182 cilofungin Proteins 0.000 description 2
ZKZKCEAHVFVZDJ-MTUMARHDSA-N cilofungin Chemical compound C1=CC(OCCCCCCCC)=CC=C1C(=O)N[C@@H]1C(=O)N[C@@H]([C@@H](C)O)C(=O)N2C[C@H](O)C[C@H]2C(=O)N[C@@H]([C@H](O)[C@@H](O)C=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)N2C[C@H](C)[C@H](O)[C@H]2C(=O)N[C@H](O)[C@H](O)C1 ZKZKCEAHVFVZDJ-MTUMARHDSA-N 0.000 description 2
229950007664 cilofungin Drugs 0.000 description 2
XVOYSCVBGLVSOL-UHFFFAOYSA-N cysteic acid Chemical compound OC(=O)C(N)CS(O)(=O)=O XVOYSCVBGLVSOL-UHFFFAOYSA-N 0.000 description 2
238000010828 elution Methods 0.000 description 2
238000006911 enzymatic reaction Methods 0.000 description 2
239000000706 filtrate Substances 0.000 description 2
230000007062 hydrolysis Effects 0.000 description 2
238000006460 hydrolysis reaction Methods 0.000 description 2
238000011081 inoculation Methods 0.000 description 2
238000012544 monitoring process Methods 0.000 description 2
238000001426 native polyacrylamide gel electrophoresis Methods 0.000 description 2
239000004323 potassium nitrate Substances 0.000 description 2
235000010333 potassium nitrate Nutrition 0.000 description 2
238000011084 recovery Methods 0.000 description 2
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
239000004317 sodium nitrate Substances 0.000 description 2
235000010344 sodium nitrate Nutrition 0.000 description 2
238000000527 sonication Methods 0.000 description 2
239000000126 substance Substances 0.000 description 2
CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 2
238000000108 ultra-filtration Methods 0.000 description 2
NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 1
108010081097 Actinoplanes utahensis deacylase Proteins 0.000 description 1
229920000936 Agarose Polymers 0.000 description 1
108091003079 Bovine Serum Albumin Proteins 0.000 description 1
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
108010013198 Daptomycin Proteins 0.000 description 1
206010017533 Fungal infection Diseases 0.000 description 1
UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
208000031888 Mycoses Diseases 0.000 description 1
GHAZCVNUKKZTLG-UHFFFAOYSA-N N-ethyl-succinimide Natural products CCN1C(=O)CCC1=O GHAZCVNUKKZTLG-UHFFFAOYSA-N 0.000 description 1
HDFGOPSGAURCEO-UHFFFAOYSA-N N-ethylmaleimide Chemical compound CCN1C(=O)C=CC1=O HDFGOPSGAURCEO-UHFFFAOYSA-N 0.000 description 1
241000589516 Pseudomonas Species 0.000 description 1
230000010933 acylation Effects 0.000 description 1
238000005917 acylation reaction Methods 0.000 description 1
238000010564 aerobic fermentation Methods 0.000 description 1
229910000147 aluminium phosphate Inorganic materials 0.000 description 1
125000000539 amino acid group Chemical group 0.000 description 1
239000003242 anti bacterial agent Substances 0.000 description 1
229940088710 antibiotic agent Drugs 0.000 description 1
239000003429 antifungal agent Substances 0.000 description 1
230000009286 beneficial effect Effects 0.000 description 1
125000003236 benzoyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C(*)=O 0.000 description 1
229940098773 bovine serum albumin Drugs 0.000 description 1
239000008366 buffered solution Substances 0.000 description 1
239000001110 calcium chloride Substances 0.000 description 1
229910001628 calcium chloride Inorganic materials 0.000 description 1
235000011148 calcium chloride Nutrition 0.000 description 1
159000000007 calcium salts Chemical class 0.000 description 1
230000015556 catabolic process Effects 0.000 description 1
238000006555 catalytic reaction Methods 0.000 description 1
239000003729 cation exchange resin Substances 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
238000012512 characterization method Methods 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
238000012258 culturing Methods 0.000 description 1
DOAKLVKFURWEDJ-QCMAZARJSA-N daptomycin Chemical compound C([C@H]1C(=O)O[C@H](C)[C@@H](C(NCC(=O)N[C@@H](CCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(=O)N[C@H](CO)C(=O)N[C@H](C(=O)N1)[C@H](C)CC(O)=O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](CC(N)=O)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)CCCCCCCCC)C(=O)C1=CC=CC=C1N DOAKLVKFURWEDJ-QCMAZARJSA-N 0.000 description 1
229960005484 daptomycin Drugs 0.000 description 1
239000007857 degradation product Substances 0.000 description 1
238000006731 degradation reaction Methods 0.000 description 1
230000008034 disappearance Effects 0.000 description 1
238000009826 distribution Methods 0.000 description 1
239000003814 drug Substances 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
238000001952 enzyme assay Methods 0.000 description 1
238000013213 extrapolation Methods 0.000 description 1
150000004665 fatty acids Chemical group 0.000 description 1
230000002349 favourable effect Effects 0.000 description 1
238000005194 fractionation Methods 0.000 description 1
PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
239000010931 gold Substances 0.000 description 1
229910052737 gold Inorganic materials 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
238000011534 incubation Methods 0.000 description 1
125000003473 lipid group Chemical group 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
239000011777 magnesium Substances 0.000 description 1
229910052749 magnesium Inorganic materials 0.000 description 1
235000001055 magnesium Nutrition 0.000 description 1
229910001629 magnesium chloride Inorganic materials 0.000 description 1
235000011147 magnesium chloride Nutrition 0.000 description 1
239000000463 material Substances 0.000 description 1
239000012528 membrane Substances 0.000 description 1
230000004048 modification Effects 0.000 description 1
238000012986 modification Methods 0.000 description 1
235000019796 monopotassium phosphate Nutrition 0.000 description 1
150000003904 phospholipids Chemical class 0.000 description 1
PJNZPQUBCPKICU-UHFFFAOYSA-N phosphoric acid;potassium Chemical compound [K].OP(O)(O)=O PJNZPQUBCPKICU-UHFFFAOYSA-N 0.000 description 1
108090000765 processed proteins & peptides Proteins 0.000 description 1
230000004952 protein activity Effects 0.000 description 1
239000012429 reaction media Substances 0.000 description 1
238000004064 recycling Methods 0.000 description 1
230000007017 scission Effects 0.000 description 1
125000004079 stearyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
230000004936 stimulating effect Effects 0.000 description 1
239000000725 suspension Substances 0.000 description 1
230000009885 systemic effect Effects 0.000 description 1
229940124597 therapeutic agent Drugs 0.000 description 1
238000010792 warming Methods 0.000 description 1
239000003643 water by type Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- C12N9/80—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in linear amides (3.5.1)
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/50—Cyclic peptides containing at least one abnormal peptide link
- C07K7/54—Cyclic peptides containing at least one abnormal peptide link with at least one abnormal peptide link in the ring
- C07K7/56—Cyclic peptides containing at least one abnormal peptide link with at least one abnormal peptide link in the ring the cyclisation not occurring through 2,4-diamino-butanoic acid
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/814—Enzyme separation or purification
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/814—Enzyme separation or purification
- Y10S435/815—Enzyme separation or purification by sorption

Landscapes

Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Bioinformatics & Cheminformatics (AREA)
Engineering & Computer Science (AREA)
Wood Science & Technology (AREA)
Zoology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Biophysics (AREA)
General Engineering & Computer Science (AREA)
Microbiology (AREA)
Biotechnology (AREA)
Biomedical Technology (AREA)
Enzymes And Modification Thereof (AREA)
Polysaccharides And Polysaccharide Derivatives (AREA)
Macromonomer-Based Addition Polymer (AREA)
Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Prostheses (AREA)
External Artificial Organs (AREA)
Orthopedics, Nursing, And Contraception (AREA)
Peptides Or Proteins (AREA)

IL9834991A 1990-06-07 1991-06-03 Diphylase lipopeptide IL98349A (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US53439490A	1990-06-07	1990-06-07

Publications (2)

Publication Number	Publication Date
IL98349A0 IL98349A0 (en)	1992-07-15
IL98349A true IL98349A (en)	1995-05-26

Family

ID=24129856

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
IL9834991A IL98349A (en)	1990-06-07	1991-06-03	Diphylase lipopeptide

Country Status (14)

Country	Link
US (1)	US5573936A (de)
EP (1)	EP0460882B1 (de)
JP (1)	JP2994486B2 (de)
KR (1)	KR0169994B1 (de)
AT (1)	ATE140728T1 (de)
CA (1)	CA2043762C (de)
DE (1)	DE69121018T2 (de)
DK (1)	DK0460882T3 (de)
ES (1)	ES2089133T3 (de)
GR (1)	GR3021292T3 (de)
HU (1)	HU215232B (de)
IE (1)	IE75885B1 (de)
IL (1)	IL98349A (de)
TW (1)	TW197471B (de)

Families Citing this family (28)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6743777B1 (en)	1992-03-19	2004-06-01	Eli Lilly And Company	Cyclic peptide antifungal agents and process for preparation thereof
ATE544851T1 (de) *	1996-03-08	2012-02-15	Astellas Pharma Inc	Verfahren zur deacylierung von zyklischen lipopeptiden
WO1997047738A1 (en) *	1996-06-13	1997-12-18	Fujisawa Pharmaceutical Co., Ltd.	Cyclic lipopeptide acylase
US6153410A (en) *	1997-03-25	2000-11-28	California Institute Of Technology	Recombination of polynucleotide sequences using random or defined primers
US6361988B1 (en)	1997-03-25	2002-03-26	California Institute Of Technology	ECB deacylase mutants
US5936074A (en) *	1997-04-17	1999-08-10	Eli Lilly And Company	Teicoplanin deacylation process and product
US6323176B1 (en)	1998-02-25	2001-11-27	Eli Lilly And Company	Cyclic peptide antifungal agents
BR9916101A (pt)	1998-12-09	2002-06-04	Lilly Co Eli	Purificação de compostos de ciclopeptìdeos equinocandinos
CA2362016A1 (en)	1999-03-03	2000-09-08	Kenneth Philip Moder	Echinocandin/carbohydrate complexes
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1991
- 1991-06-03 AT AT91304976T patent/ATE140728T1/de not_active IP Right Cessation
- 1991-06-03 DK DK91304976.3T patent/DK0460882T3/da active
- 1991-06-03 CA CA002043762A patent/CA2043762C/en not_active Expired - Fee Related
- 1991-06-03 EP EP91304976A patent/EP0460882B1/de not_active Expired - Lifetime
- 1991-06-03 ES ES91304976T patent/ES2089133T3/es not_active Expired - Lifetime
- 1991-06-03 DE DE69121018T patent/DE69121018T2/de not_active Expired - Fee Related
- 1991-06-03 IL IL9834991A patent/IL98349A/en not_active IP Right Cessation
- 1991-06-04 JP JP3132622A patent/JP2994486B2/ja not_active Expired - Fee Related
- 1991-06-05 KR KR1019910009280A patent/KR0169994B1/ko not_active Expired - Fee Related
- 1991-06-06 IE IE193991A patent/IE75885B1/en not_active IP Right Cessation
- 1991-06-06 HU HU911897A patent/HU215232B/hu not_active IP Right Cessation
- 1991-06-06 TW TW080104442A patent/TW197471B/zh active
1995
- 1995-05-18 US US08/444,126 patent/US5573936A/en not_active Expired - Fee Related
1996
- 1996-10-09 GR GR960402663T patent/GR3021292T3/el unknown

Also Published As

Publication number	Publication date
DE69121018D1 (de)	1996-08-29
KR0169994B1 (ko)	1999-02-01
CA2043762A1 (en)	1991-12-08
IE75885B1 (en)	1997-09-24
TW197471B (de)	1993-01-01
JP2994486B2 (ja)	1999-12-27
DK0460882T3 (da)	1996-08-26
GR3021292T3 (en)	1997-01-31
ES2089133T3 (es)	1996-10-01
IL98349A0 (en)	1992-07-15
US5573936A (en)	1996-11-12
EP0460882A3 (en)	1992-04-22
DE69121018T2 (de)	1996-12-19
IE911939A1 (en)	1991-12-18
HUT61587A (en)	1993-01-28
HU215232B (hu)	1998-11-30
EP0460882A2 (de)	1991-12-11
KR920000919A (ko)	1992-01-29
ATE140728T1 (de)	1996-08-15
CA2043762C (en)	2001-05-29
EP0460882B1 (de)	1996-07-24
HU911897D0 (en)	1991-12-30
JPH04228072A (ja)	1992-08-18

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Date	Code	Title
1997-11-20	KB	Patent renewed
2001-07-24	KB	Patent renewed
2006-03-12	MM9K	Patent not in force due to non-payment of renewal fees

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