ES2702786T3 - Procedimiento de síntesis de proteínas - Google Patents
Procedimiento de síntesis de proteínas Download PDFInfo
- Publication number
- ES2702786T3 ES2702786T3 ES12772951T ES12772951T ES2702786T3 ES 2702786 T3 ES2702786 T3 ES 2702786T3 ES 12772951 T ES12772951 T ES 12772951T ES 12772951 T ES12772951 T ES 12772951T ES 2702786 T3 ES2702786 T3 ES 2702786T3
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- peptide
- thiol
- seaoff
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- Prior art date
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- UENWRTRMUIOCKN-UHFFFAOYSA-N benzyl thiol Chemical compound SCC1=CC=CC=C1 UENWRTRMUIOCKN-UHFFFAOYSA-N 0.000 description 1
- 125000003917 carbamoyl group Chemical group [H]N([H])C(*)=O 0.000 description 1
- 150000001732 carboxylic acid derivatives Chemical group 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 238000001311 chemical methods and process Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- JZCCFEFSEZPSOG-UHFFFAOYSA-L copper(II) sulfate pentahydrate Chemical compound O.O.O.O.O.[Cu+2].[O-]S([O-])(=O)=O JZCCFEFSEZPSOG-UHFFFAOYSA-L 0.000 description 1
- 238000006352 cycloaddition reaction Methods 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 238000006114 decarboxylation reaction Methods 0.000 description 1
- 238000006477 desulfuration reaction Methods 0.000 description 1
- 230000023556 desulfurization Effects 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 239000003344 environmental pollutant Substances 0.000 description 1
- 229940031098 ethanolamine Drugs 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 238000007306 functionalization reaction Methods 0.000 description 1
- GTFMAONWNTUZEW-UHFFFAOYSA-N glutaramic acid Chemical compound NC(=O)CCCC(O)=O GTFMAONWNTUZEW-UHFFFAOYSA-N 0.000 description 1
- VANNPISTIUFMLH-UHFFFAOYSA-N glutaric anhydride Chemical compound O=C1CCCC(=O)O1 VANNPISTIUFMLH-UHFFFAOYSA-N 0.000 description 1
- 125000003827 glycol group Chemical group 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 229920000578 graft copolymer Polymers 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 150000004715 keto acids Chemical class 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- WQEPLUUGTLDZJY-UHFFFAOYSA-N n-Pentadecanoic acid Natural products CCCCCCCCCCCCCCC(O)=O WQEPLUUGTLDZJY-UHFFFAOYSA-N 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 125000000962 organic group Chemical group 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000011049 pearl Substances 0.000 description 1
- MINRDQDGBLQBGD-UHFFFAOYSA-N pent-2-ynoic acid Chemical compound CCC#CC(O)=O MINRDQDGBLQBGD-UHFFFAOYSA-N 0.000 description 1
- 239000000863 peptide conjugate Substances 0.000 description 1
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
- 150000003003 phosphines Chemical class 0.000 description 1
- 229910000073 phosphorus hydride Inorganic materials 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 231100000719 pollutant Toxicity 0.000 description 1
- 239000002952 polymeric resin Substances 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000004224 protection Effects 0.000 description 1
- 150000003254 radicals Chemical class 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 235000010378 sodium ascorbate Nutrition 0.000 description 1
- PPASLZSBLFJQEF-RKJRWTFHSA-M sodium ascorbate Substances [Na+].OC[C@@H](O)[C@H]1OC(=O)C(O)=C1[O-] PPASLZSBLFJQEF-RKJRWTFHSA-M 0.000 description 1
- 229960005055 sodium ascorbate Drugs 0.000 description 1
- PPASLZSBLFJQEF-RXSVEWSESA-M sodium-L-ascorbate Chemical compound [Na+].OC[C@H](O)[C@H]1OC(=O)C(O)=C1[O-] PPASLZSBLFJQEF-RXSVEWSESA-M 0.000 description 1
- UIIMBOGNXHQVGW-UHFFFAOYSA-N sodium;hydron;carbonate Chemical compound [Na+].OC(O)=O UIIMBOGNXHQVGW-UHFFFAOYSA-N 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 230000019635 sulfation Effects 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- 125000000020 sulfo group Chemical group O=S(=O)([*])O[H] 0.000 description 1
- 230000000153 supplemental effect Effects 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 229920003002 synthetic resin Polymers 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 125000004213 tert-butoxy group Chemical group [H]C([H])([H])C(O*)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- WGTODYJZXSJIAG-UHFFFAOYSA-N tetramethylrhodamine chloride Chemical compound [Cl-].C=12C=CC(N(C)C)=CC2=[O+]C2=CC(N(C)C)=CC=C2C=1C1=CC=CC=C1C(O)=O WGTODYJZXSJIAG-UHFFFAOYSA-N 0.000 description 1
- 230000001256 tonic effect Effects 0.000 description 1
- 238000006257 total synthesis reaction Methods 0.000 description 1
- 230000017105 transposition Effects 0.000 description 1
- DTQVDTLACAAQTR-UHFFFAOYSA-N trifluoroacetic acid Substances OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 1
- 230000034512 ubiquitination Effects 0.000 description 1
- 238000010798 ubiquitination Methods 0.000 description 1
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 description 1
- 125000005500 uronium group Chemical group 0.000 description 1
- 229960005486 vaccine Drugs 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/1072—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups
- C07K1/1077—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups by covalent attachment of residues other than amino acids or peptide residues, e.g. sugars, polyols, fatty acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/02—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length in solution
- C07K1/026—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length in solution by fragment condensation in solution
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/04—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/04—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers
- C07K1/042—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers characterised by the nature of the carrier
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/04—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers
- C07K1/045—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers using devices to improve synthesis, e.g. reactors, special vessels
-
- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08F—MACROMOLECULAR COMPOUNDS OBTAINED BY REACTIONS ONLY INVOLVING CARBON-TO-CARBON UNSATURATED BONDS
- C08F8/00—Chemical modification by after-treatment
- C08F8/34—Introducing sulfur atoms or sulfur-containing groups
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Polymers & Plastics (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FR1159348A FR2981352B1 (fr) | 2011-10-17 | 2011-10-17 | Procede de synthese de proteines |
| PCT/EP2012/070454 WO2013057084A1 (fr) | 2011-10-17 | 2012-10-16 | Procede de synthese de proteines |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2702786T3 true ES2702786T3 (es) | 2019-03-05 |
Family
ID=47022687
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES12772951T Active ES2702786T3 (es) | 2011-10-17 | 2012-10-16 | Procedimiento de síntesis de proteínas |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US9206224B2 (enExample) |
| EP (1) | EP2768842B1 (enExample) |
| JP (1) | JP6321542B2 (enExample) |
| CN (1) | CN103998455B (enExample) |
| CA (1) | CA2852833A1 (enExample) |
| ES (1) | ES2702786T3 (enExample) |
| FR (1) | FR2981352B1 (enExample) |
| IN (1) | IN2014CN02870A (enExample) |
| SG (1) | SG11201401540WA (enExample) |
| WO (1) | WO2013057084A1 (enExample) |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2971509B1 (fr) * | 2011-02-16 | 2013-02-22 | Centre Nat Rech Scient | Procede de preparation de peptides par assemblage de multiples fragments peptidiques |
| AU2014286990A1 (en) | 2013-07-11 | 2016-02-11 | Novartis Ag | Lysine-specific chemoenzymatic protein modifications using microbial transglutaminase |
| NL2027769B1 (en) * | 2021-03-18 | 2022-09-29 | Univ Delft Tech | C-terminal peptide modification |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK0832096T3 (da) | 1995-05-04 | 2001-10-01 | Scripps Research Inst | Syntese af proteiner ved nativ kemisk ligering |
| WO1998028434A1 (en) | 1996-12-24 | 1998-07-02 | The Scripps Research Institute | General chemical ligation |
| AU745094B2 (en) * | 1997-06-13 | 2002-03-14 | Gryphon Sciences | Solid phase native chemical ligation of unprotected or N-terminal cysteine protected peptides in aqueous solution |
| AU2001281463A1 (en) | 2000-03-16 | 2001-09-24 | The Regents Of The University Of California | Chemoselective ligation |
| AU2001261530B2 (en) | 2000-05-12 | 2006-11-09 | Wisconsin Alumni Research Foundation | Ligation method and reagents to form an amide bond |
| CA2466746A1 (en) | 2001-11-14 | 2003-05-22 | Geneprot, Inc. | Extended native chemical ligation of three or more peptide fragments |
| TW200637872A (en) * | 2004-10-26 | 2006-11-01 | Lonza Ag | Thiol group protection and cyclization in solid-phase peptide synthesis |
| JP5139085B2 (ja) * | 2005-02-11 | 2013-02-06 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフツング | 固相のオリゴ糖タグ付け：固定化糖質の操作技術 |
| US7667076B2 (en) | 2005-09-14 | 2010-02-23 | Regents Of The University Of California | Amide forming chemical ligation |
| FR2952058B1 (fr) * | 2009-10-29 | 2013-10-04 | Centre Nat Rech Scient | Procede de ligation native de polypeptides |
| EP2501711B1 (en) | 2009-11-16 | 2014-01-08 | Centre National De La Recherche Scientifique CNRS | Compounds and methods for purifying peptides produced by solid phase peptide synthesis |
-
2011
- 2011-10-17 FR FR1159348A patent/FR2981352B1/fr not_active Expired - Fee Related
-
2012
- 2012-10-16 SG SG11201401540WA patent/SG11201401540WA/en unknown
- 2012-10-16 ES ES12772951T patent/ES2702786T3/es active Active
- 2012-10-16 JP JP2014536201A patent/JP6321542B2/ja active Active
- 2012-10-16 IN IN2870CHN2014 patent/IN2014CN02870A/en unknown
- 2012-10-16 CA CA2852833A patent/CA2852833A1/fr not_active Abandoned
- 2012-10-16 EP EP12772951.5A patent/EP2768842B1/fr not_active Not-in-force
- 2012-10-16 CN CN201280062427.3A patent/CN103998455B/zh not_active Expired - Fee Related
- 2012-10-16 WO PCT/EP2012/070454 patent/WO2013057084A1/fr not_active Ceased
- 2012-10-16 US US14/352,155 patent/US9206224B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| CN103998455B (zh) | 2018-05-29 |
| US9206224B2 (en) | 2015-12-08 |
| SG11201401540WA (en) | 2014-06-27 |
| EP2768842A1 (fr) | 2014-08-27 |
| WO2013057084A1 (fr) | 2013-04-25 |
| FR2981352B1 (fr) | 2015-07-03 |
| EP2768842B1 (fr) | 2018-07-25 |
| FR2981352A1 (fr) | 2013-04-19 |
| JP2014532075A (ja) | 2014-12-04 |
| CA2852833A1 (fr) | 2013-04-25 |
| US20140256879A1 (en) | 2014-09-11 |
| JP6321542B2 (ja) | 2018-05-09 |
| IN2014CN02870A (enExample) | 2015-07-03 |
| CN103998455A (zh) | 2014-08-20 |
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