NL8020143A - Cyclisch analoog van in de natuur voorkomend fagocytosis stimulerend peptide-threonyl-cyclo -n epsilon-lysyl-prolyl-arginyl. - Google Patents

Cyclisch analoog van in de natuur voorkomend fagocytosis stimulerend peptide-threonyl-cyclo -n epsilon-lysyl-prolyl-arginyl. Download PDF

Info

Publication number: NL8020143A
Authority: NL; Netherlands
Prior art keywords: prolyl; lysyl; threonyl; cyclo; arginyl
Prior art date: 1979-04-02

Application number

NL8020143A

Other languages

English (en)

Dutch (nl)

Original Assignee

Inst Organicheskogo Sinteza Ak

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.)

1979-04-02

Filing date

1980-04-02

Publication date

1981-02-27

1980-04-02 Application filed by Inst Organicheskogo Sinteza Ak filed Critical Inst Organicheskogo Sinteza Ak

1981-02-27 Publication of NL8020143A publication Critical patent/NL8020143A/nl

Links

230000004936 stimulating effect Effects 0.000 title description 7
206010057249 Phagocytosis Diseases 0.000 title description 6
230000008782 phagocytosis Effects 0.000 title description 6
ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 claims description 18
230000015572 biosynthetic process Effects 0.000 claims description 5
125000004122 cyclic group Chemical group 0.000 claims description 5
238000003786 synthesis reaction Methods 0.000 claims description 5
125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 claims description 5
JXGVXCZADZNAMJ-NSHDSACASA-N (2s)-1-phenylmethoxycarbonylpyrrolidine-2-carboxylic acid Chemical compound OC(=O)[C@@H]1CCCN1C(=O)OCC1=CC=CC=C1 JXGVXCZADZNAMJ-NSHDSACASA-N 0.000 claims description 4
LLHOYOCAAURYRL-RITPCOANSA-N (2s,3r)-3-hydroxy-2-[(2-methylpropan-2-yl)oxycarbonylamino]butanoic acid Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)OC(C)(C)C LLHOYOCAAURYRL-RITPCOANSA-N 0.000 claims description 4
244000186140 Asperula odorata Species 0.000 claims description 4
235000008526 Galium odoratum Nutrition 0.000 claims description 4
239000003153 chemical reaction reagent Substances 0.000 claims description 4
YXGMZBUOYWYJAH-HNNXBMFYSA-N (2s)-6-amino-2-[(2-methylpropan-2-yl)oxycarbonyl-phenylmethoxycarbonylamino]hexanoic acid Chemical compound NCCCC[C@@H](C(O)=O)N(C(=O)OC(C)(C)C)C(=O)OCC1=CC=CC=C1 YXGMZBUOYWYJAH-HNNXBMFYSA-N 0.000 claims description 3
102100029251 Phagocytosis-stimulating peptide Human genes 0.000 claims description 3
101710177686 Phagocytosis-stimulating peptide Proteins 0.000 claims description 3
108090000765 processed proteins & peptides Proteins 0.000 claims description 3
229910052799 carbon Inorganic materials 0.000 claims description 2
125000004432 carbon atom Chemical group C* 0.000 claims description 2
150000002170 ethers Chemical class 0.000 claims description 2
238000000926 separation method Methods 0.000 claims description 2
238000004519 manufacturing process Methods 0.000 claims 1
238000006798 ring closing metathesis reaction Methods 0.000 claims 1
239000000243 solution Substances 0.000 description 18
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 17
150000001875 compounds Chemical class 0.000 description 16
RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 14
239000000047 product Substances 0.000 description 11
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 9
230000000242 pagocytic effect Effects 0.000 description 9
230000000694 effects Effects 0.000 description 8
-1 tert-butyloxycarbonyl-threonyl-N-benzyloxycarbonyl-lysyl-prolyl-arginine Chemical compound 0.000 description 8
HMNSRTLZAJHSIK-YUMQZZPRSA-N Pro-Arg Chemical compound NC(=N)NCCC[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1 HMNSRTLZAJHSIK-YUMQZZPRSA-N 0.000 description 7
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XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 6
210000000440 neutrophil Anatomy 0.000 description 6
108010004914 prolylarginine Proteins 0.000 description 6
JHLYAZHQNOZKSJ-BCYZHJNNSA-N (2s)-2-[[(2s)-1-[(2s)-6-amino-2-[[(2s,3r)-3-hydroxy-2-[(2-methylpropan-2-yl)oxycarbonylamino]butanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-5-(diaminomethylideneamino)pentanoic acid Chemical compound CC(C)(C)OC(=O)N[C@@H]([C@H](O)C)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCN=C(N)N)C(O)=O JHLYAZHQNOZKSJ-BCYZHJNNSA-N 0.000 description 5
CPELXLSAUQHCOX-UHFFFAOYSA-N Hydrogen bromide Chemical compound Br CPELXLSAUQHCOX-UHFFFAOYSA-N 0.000 description 5
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XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 4
239000004475 Arginine Substances 0.000 description 4
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DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 4
239000012362 glacial acetic acid Substances 0.000 description 4
239000011541 reaction mixture Substances 0.000 description 4
239000002904 solvent Substances 0.000 description 4
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GURXTMUZBXIKPA-GJZGRUSLSA-N (2s)-5-(diaminomethylideneazaniumyl)-2-[[(2s)-1-phenylmethoxycarbonylpyrrolidine-2-carbonyl]amino]pentanoate Chemical compound NC(=N)NCCC[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)OCC1=CC=CC=C1 GURXTMUZBXIKPA-GJZGRUSLSA-N 0.000 description 3
QJHMHZVVRVXKOY-UHFFFAOYSA-N 1,2,3,4,5-pentafluoro-6-(2,3,4,5,6-pentafluorophenoxy)benzene Chemical compound FC1=C(F)C(F)=C(F)C(F)=C1OC1=C(F)C(F)=C(F)C(F)=C1F QJHMHZVVRVXKOY-UHFFFAOYSA-N 0.000 description 3
KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 3
ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 3
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238000002844 melting Methods 0.000 description 3
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PNCBNJDEBRZFAI-UFYCRDLUSA-N (2s)-2-[[(2s)-1-[(2s)-6-amino-2-(phenylmethoxycarbonylamino)hexanoyl]pyrrolidine-2-carbonyl]amino]-5-(diaminomethylideneamino)pentanoic acid Chemical compound N([C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)C(=O)OCC1=CC=CC=C1 PNCBNJDEBRZFAI-UFYCRDLUSA-N 0.000 description 2
MWAGUKZCDDRDCS-UHFFFAOYSA-N 1-nitro-4-(4-nitrophenoxy)benzene Chemical compound C1=CC([N+](=O)[O-])=CC=C1OC1=CC=C([N+]([O-])=O)C=C1 MWAGUKZCDDRDCS-UHFFFAOYSA-N 0.000 description 2
241000894006 Bacteria Species 0.000 description 2
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
230000009471 action Effects 0.000 description 2
150000001413 amino acids Chemical class 0.000 description 2
238000006243 chemical reaction Methods 0.000 description 2
239000003814 drug Substances 0.000 description 2
230000002255 enzymatic effect Effects 0.000 description 2
HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
229910000042 hydrogen bromide Inorganic materials 0.000 description 2
IXCSERBJSXMMFS-UHFFFAOYSA-N hydrogen chloride Substances Cl.Cl IXCSERBJSXMMFS-UHFFFAOYSA-N 0.000 description 2
229910000041 hydrogen chloride Inorganic materials 0.000 description 2
229960001438 immunostimulant agent Drugs 0.000 description 2
239000003022 immunostimulating agent Substances 0.000 description 2
230000003308 immunostimulating effect Effects 0.000 description 2
238000000338 in vitro Methods 0.000 description 2
210000002540 macrophage Anatomy 0.000 description 2
125000000896 monocarboxylic acid group Chemical group 0.000 description 2
230000004899 motility Effects 0.000 description 2
235000016709 nutrition Nutrition 0.000 description 2
230000035764 nutrition Effects 0.000 description 2
238000002360 preparation method Methods 0.000 description 2
238000001953 recrystallisation Methods 0.000 description 2
239000000741 silica gel Substances 0.000 description 2
229910002027 silica gel Inorganic materials 0.000 description 2
IESDGNYHXIOKRW-YXMSTPNBSA-N (2s)-2-[[(2s)-1-[(2s)-6-amino-2-[[(2s,3r)-2-amino-3-hydroxybutanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-5-(diaminomethylideneamino)pentanoic acid Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(N)=N)C(O)=O IESDGNYHXIOKRW-YXMSTPNBSA-N 0.000 description 1
CDAOWUNZBZEBDA-UHFFFAOYSA-N 1-fluoro-2-(2-fluorophenoxy)benzene Chemical compound FC1=CC=CC=C1OC1=CC=CC=C1F CDAOWUNZBZEBDA-UHFFFAOYSA-N 0.000 description 1
USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
239000005695 Ammonium acetate Substances 0.000 description 1
102000003670 Carboxypeptidase B Human genes 0.000 description 1
108090000087 Carboxypeptidase B Proteins 0.000 description 1
KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
208000035473 Communicable disease Diseases 0.000 description 1
102000004190 Enzymes Human genes 0.000 description 1
108090000790 Enzymes Proteins 0.000 description 1
238000012404 In vitro experiment Methods 0.000 description 1
239000004472 Lysine Substances 0.000 description 1
KDLHZDBZIXYQEI-UHFFFAOYSA-N Palladium Chemical compound [Pd] KDLHZDBZIXYQEI-UHFFFAOYSA-N 0.000 description 1
208000008425 Protein deficiency Diseases 0.000 description 1
241000191967 Staphylococcus aureus Species 0.000 description 1
YKRQRPFODDJQTC-CSMHCCOUSA-N Thr-Lys Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@H](C(O)=O)CCCCN YKRQRPFODDJQTC-CSMHCCOUSA-N 0.000 description 1
DTQVDTLACAAQTR-UHFFFAOYSA-M Trifluoroacetate Chemical compound [O-]C(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-M 0.000 description 1
108700017376 Tuftsin Deficiency Proteins 0.000 description 1
208000002581 Tuftsin deficiency Diseases 0.000 description 1
230000004913 activation Effects 0.000 description 1
229940093740 amino acid and derivative Drugs 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
230000004071 biological effect Effects 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
239000008280 blood Substances 0.000 description 1
230000023555 blood coagulation Effects 0.000 description 1
210000004899 c-terminal region Anatomy 0.000 description 1
210000004027 cell Anatomy 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
238000004587 chromatography analysis Methods 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
238000010276 construction Methods 0.000 description 1
238000001816 cooling Methods 0.000 description 1
238000012937 correction Methods 0.000 description 1
230000003247 decreasing effect Effects 0.000 description 1
YWEUIGNSBFLMFL-UHFFFAOYSA-N diphosphonate Chemical compound O=P(=O)OP(=O)=O YWEUIGNSBFLMFL-UHFFFAOYSA-N 0.000 description 1
201000010099 disease Diseases 0.000 description 1
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
238000000921 elemental analysis Methods 0.000 description 1
230000007071 enzymatic hydrolysis Effects 0.000 description 1
238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
PSLIMVZEAPALCD-UHFFFAOYSA-N ethanol;ethoxyethane Chemical compound CCO.CCOCC PSLIMVZEAPALCD-UHFFFAOYSA-N 0.000 description 1
NLFBCYMMUAKCPC-KQQUZDAGSA-N ethyl (e)-3-[3-amino-2-cyano-1-[(e)-3-ethoxy-3-oxoprop-1-enyl]sulfanyl-3-oxoprop-1-enyl]sulfanylprop-2-enoate Chemical compound CCOC(=O)\C=C\SC(=C(C#N)C(N)=O)S\C=C\C(=O)OCC NLFBCYMMUAKCPC-KQQUZDAGSA-N 0.000 description 1
125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 1
238000001704 evaporation Methods 0.000 description 1
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238000002474 experimental method Methods 0.000 description 1
235000013305 food Nutrition 0.000 description 1
239000012634 fragment Substances 0.000 description 1
230000007062 hydrolysis Effects 0.000 description 1
238000006460 hydrolysis reaction Methods 0.000 description 1
230000028993 immune response Effects 0.000 description 1
230000002163 immunogen Effects 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
230000005764 inhibitory process Effects 0.000 description 1
230000003993 interaction Effects 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
230000033001 locomotion Effects 0.000 description 1
239000000463 material Substances 0.000 description 1
229910052757 nitrogen Inorganic materials 0.000 description 1
230000001717 pathogenic effect Effects 0.000 description 1
208000025712 phagocytic cell dysfunction Diseases 0.000 description 1
239000008177 pharmaceutical agent Substances 0.000 description 1
DLYUQMMRRRQYAE-UHFFFAOYSA-N phosphorus pentoxide Inorganic materials O1P(O2)(=O)OP3(=O)OP1(=O)OP2(=O)O3 DLYUQMMRRRQYAE-UHFFFAOYSA-N 0.000 description 1
239000000843 powder Substances 0.000 description 1
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238000000746 purification Methods 0.000 description 1
238000007363 ring formation reaction Methods 0.000 description 1
230000009476 short term action Effects 0.000 description 1
239000011780 sodium chloride Substances 0.000 description 1
238000010911 splenectomy Methods 0.000 description 1
208000027140 splenic disease Diseases 0.000 description 1
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239000000725 suspension Substances 0.000 description 1
208000011580 syndromic disease Diseases 0.000 description 1
125000005931 tert-butyloxycarbonyl group Chemical group [H]C([H])([H])C(OC(*)=O)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
229940126585 therapeutic drug Drugs 0.000 description 1
238000004809 thin layer chromatography Methods 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/02—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing at least one abnormal peptide link
- C07K5/0215—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing at least one abnormal peptide link containing natural amino acids, forming a peptide bond via their side chain functional group, e.g. epsilon-Lys, gamma-Glu
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1002—Tetrapeptides with the first amino acid being neutral
- C07K5/1005—Tetrapeptides with the first amino acid being neutral and aliphatic
- C07K5/1013—Tetrapeptides with the first amino acid being neutral and aliphatic the side chain containing O or S as heteroatoms, e.g. Cys, Ser
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- 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
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/27—Cyclic peptide or cyclic protein

Landscapes

Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Health & Medical Sciences (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Molecular Biology (AREA)
Genetics & Genomics (AREA)
Biophysics (AREA)
Biochemistry (AREA)
Immunology (AREA)
Pharmacology & Pharmacy (AREA)
Animal Behavior & Ethology (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Bioinformatics & Cheminformatics (AREA)
Engineering & Computer Science (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Peptides Or Proteins (AREA)

NL8020143A 1979-04-02 1980-04-02 Cyclisch analoog van in de natuur voorkomend fagocytosis stimulerend peptide-threonyl-cyclo -n epsilon-lysyl-prolyl-arginyl. NL8020143A (nl)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
SU2744960		1979-02-04
SU2744960		1979-04-02

Publications (1)

Publication Number	Publication Date
NL8020143A true NL8020143A (nl)	1981-02-27

Family

ID=20818742

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NL8020143A NL8020143A (nl)	1979-04-02	1980-04-02	Cyclisch analoog van in de natuur voorkomend fagocytosis stimulerend peptide-threonyl-cyclo -n epsilon-lysyl-prolyl-arginyl.

Country Status (11)

Country	Link
US (1)	US4434095A (da)
JP (1)	JPS5811426B2 (da)
BE (1)	BE882602A (da)
DK (1)	DK513880A (da)
FR (1)	FR2453136A1 (da)
GB (1)	GB2058085B (da)
IT (1)	IT8021120A0 (da)
NL (1)	NL8020143A (da)
NO (1)	NO803623L (da)
SE (1)	SE8008415L (da)
WO (1)	WO1980002141A1 (da)

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* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS59186947A (ja) *	1983-03-09	1984-10-23	Kowa Co	新規ペプチド
FR2601957B1 (fr) *	1986-07-22	1988-11-10	Pf Medicament	Derives tetrapeptidiques, procede pour leur preparation, leur utilisation en tant que medicaments et compositions pharmaceutiques obtenues
FR2610934B1 (fr) *	1987-02-13	1989-05-05	Adir	Nouveaux derives peptidiques a structure polycyclique azotee, leur procede de preparation et les compositions pharmaceutiques qui les contiennent
FR2616663B1 (fr) *	1987-06-16	1989-08-18	Adir	Nouveaux tripeptides a structure polycyclique azotee, leur procede de preparation et les compositions pharmaceutiques qui les contiennent
DE68923572T2 (de) *	1988-03-28	1996-01-18	British Tech Group	Peptide.
GB8807427D0 (en) *	1988-03-28	1988-05-05	National Biological Standards Board	Peptides
US5028593A (en) *	1989-08-15	1991-07-02	Board Of Regents, The University Of Texas System	Tuftsin analogs
EP0454302A3 (en) *	1990-03-30	1992-10-14	Banyu Pharmaceutical Co., Ltd.	Tuftsin derivatives
US6177405B1 (en) *	1992-07-22	2001-01-23	Kenji Nishioka	Cyclic analogs of tuftsin
US5569745A (en) *	1994-02-25	1996-10-29	Resolution Pharmaceuticals Inc.	Peptide-Chelator conjugates
US8039026B1 (en) *	1997-07-28	2011-10-18	Johnson & Johnson Consumer Companies, Inc	Methods for treating skin pigmentation
US8093293B2 (en) *	1998-07-06	2012-01-10	Johnson & Johnson Consumer Companies, Inc.	Methods for treating skin conditions
US8106094B2 (en) *	1998-07-06	2012-01-31	Johnson & Johnson Consumer Companies, Inc.	Compositions and methods for treating skin conditions
US20020197244A1 (en) *	1998-12-07	2002-12-26	Miri Seiberg	Compositions and methods for regulating phagocytosis and ICAM-1 expression
US7985404B1 (en)	1999-07-27	2011-07-26	Johnson & Johnson Consumer Companies, Inc.	Reducing hair growth, hair follicle and hair shaft size and hair pigmentation
US7309688B2 (en)	2000-10-27	2007-12-18	Johnson & Johnson Consumer Companies	Topical anti-cancer compositions and methods of use thereof
US8431550B2 (en) *	2000-10-27	2013-04-30	Johnson & Johnson Consumer Companies, Inc.	Topical anti-cancer compositions and methods of use thereof
US7192615B2 (en) *	2001-02-28	2007-03-20	J&J Consumer Companies, Inc.	Compositions containing legume products
US20030224075A1 (en) *	2002-02-21	2003-12-04	Jue-Chen Liu	Soy composition for balancing combination skin
US20050004561A1 (en) *	2003-07-01	2005-01-06	Lynn Halas	Method for removing hair
KR20060125746A (ko) *	2003-10-29	2006-12-06	죤슨 앤 죤슨 컨슈머 프랑스 에스에이에스	대두 제품과 이산을 포함한 조성물
US20080008818A1 (en) *	2006-06-23	2008-01-10	Miri Seiberg	Partially denatured whole soybean extracts and methods of use thereof
US20080089960A1 (en) *	2006-10-16	2008-04-17	Miri Seiberg	Use of Legume Products for the Treatment and Prevention of Radiotherapy-Induced Skin Damage

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US3778426A (en) *	1970-12-16	1973-12-11	Research Corp	Therapeutically useful polypeptides

1980
- 1980-04-01 IT IT8021120A patent/IT8021120A0/it unknown
- 1980-04-02 JP JP55500900A patent/JPS5811426B2/ja not_active Expired
- 1980-04-02 NL NL8020143A patent/NL8020143A/nl not_active Application Discontinuation
- 1980-04-02 GB GB8038342A patent/GB2058085B/en not_active Expired
- 1980-04-02 WO PCT/SU1980/000060 patent/WO1980002141A1/ru not_active Ceased
- 1980-04-02 US US06/227,055 patent/US4434095A/en not_active Expired - Fee Related
- 1980-04-02 FR FR8007504A patent/FR2453136A1/fr active Granted
- 1980-04-02 BE BE0/200092A patent/BE882602A/fr not_active IP Right Cessation
- 1980-12-01 NO NO803623A patent/NO803623L/no unknown
- 1980-12-01 SE SE8008415A patent/SE8008415L/xx not_active Application Discontinuation
- 1980-12-02 DK DK513880A patent/DK513880A/da not_active Application Discontinuation

Also Published As

Publication number	Publication date
NO803623L (no)	1980-12-01
WO1980002141A1 (fr)	1980-10-16
FR2453136B1 (da)	1983-03-11
BE882602A (fr)	1980-10-02
GB2058085B (en)	1983-01-26
DK513880A (da)	1980-12-02
JPS56500340A (da)	1981-03-19
GB2058085A (en)	1981-04-08
FR2453136A1 (fr)	1980-10-31
JPS5811426B2 (ja)	1983-03-02
US4434095A (en)	1984-02-28
SE8008415L (sv)	1980-12-01
IT8021120A0 (it)	1980-04-01

Legal Events

Date	Code	Title
1981-03-10	A1A	A request for search or an international-type search has been filed
1981-09-01	BB	A search report has been drawn up
1982-02-01	BC	A request for examination has been filed
1985-01-01	A85	Still pending on 85-01-01
1985-12-02	BV	The patent application has lapsed

Publication	Publication Date	Title
NL8020143A (nl)	1981-02-27	Cyclisch analoog van in de natuur voorkomend fagocytosis stimulerend peptide-threonyl-cyclo -n epsilon-lysyl-prolyl-arginyl.
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DE68913935T2 (de)	1994-07-07	Verfahren zur Herstellung von Retro-Inverso-Peptiden und dessen Zwischenprodukte.
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JPH05508394A (ja)	1993-11-25	新規なｃｃ―１０６５アナログ
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Harris et al.	1950	The synthesis of peptides related to gramicidin S and the significance of optical configuration in antibiotic peptides. 2. Pentapeptides
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DE69119185T2 (de)	1996-08-14	Derivate von Carboxymethyl-Chitin und ihre Verwendung
RU2026302C1 (ru)	1995-01-09	Способ получения n-алкилпроизводных антибиотиков или их фармацевтически приемлемых солей
Bloom et al.	1966	The Synthesis of Glycyl-L-prolylglycyl and Glycyl-L-prolyl-L-alanyl Oligopeptides and Sequential Polypeptides1
EP0292729B1 (de)	1992-04-22	Neue Festphasen-Peptidsynthesemethoden
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DE1248059B (de)	1967-08-24	Verfahren zur Herstellung bradykininwirksamer Undeca- und Dodecapeptide
Blagodarov et al.	2022	Improving the synthesis of hemin derivatives and their effect on bacterial biofilms
Rocchi et al.	1969	Synthesis of peptide analogs of the N-terminal eicosapeptide sequence of ribonuclease A. XI. Synthesis and conformational studies of [Orn10, Nle13]-S-peptide
EP2958934B1 (en)	2016-10-05	Peptidomimetics possessing photo-controlled biological activity
Yamada et al.	1990	Nα-acetylhistidine metabolism in fish—I. Identification of Nα-acetylhistidine in the heart of rainbow trout Salmo gairdneri
Kumara et al.	2018	Dipeptides as linker for multicomponent presentation—A facile, robust, and high-bioactivity yielding strategy
US3752800A (en)	1973-08-14	Process for the manufacture of a pyroglutamylpeptide
DE4214328A1 (de)	1992-11-05	Neue peptidderivate die als inhibitoren von bakteriellen kollagenasen verwendet werden koennen
SU784218A1 (ru)	1981-09-07	Синтетический аналог природного пептида тафцина, обладающий фагоцитозстимулирующей активностью