IL265236B2 - Multipurpose medical buildings and their uses - Google Patents
Multipurpose medical buildings and their usesInfo
- Publication number
- IL265236B2 IL265236B2 IL265236A IL26523619A IL265236B2 IL 265236 B2 IL265236 B2 IL 265236B2 IL 265236 A IL265236 A IL 265236A IL 26523619 A IL26523619 A IL 26523619A IL 265236 B2 IL265236 B2 IL 265236B2
- Authority
- IL
- Israel
- Prior art keywords
- toxin
- peptide
- peptides
- seq
- construct
- Prior art date
Links
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- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4748—Tumour specific antigens; Tumour rejection antigen precursors [TRAP], e.g. MAGE
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- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70503—Immunoglobulin superfamily
- C07K14/70532—B7 molecules, e.g. CD80, CD86
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- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/82—Translation products from oncogenes
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- 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
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/33—Fusion polypeptide fusions for targeting to specific cell types, e.g. tissue specific targeting, targeting of a bacterial subspecies
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/40—Fusion polypeptide containing a tag for immunodetection, or an epitope for immunisation
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/55—Fusion polypeptide containing a fusion with a toxin, e.g. diphteria toxin
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
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- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Oncology (AREA)
- Cell Biology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (3)
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| US201662401192P | 2016-09-29 | 2016-09-29 | |
| US201662401195P | 2016-09-29 | 2016-09-29 | |
| PCT/IL2017/051094 WO2018061004A1 (en) | 2016-09-29 | 2017-09-27 | Therapeutic multi-targeting constructs and uses thereof |
Publications (3)
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| IL265236A IL265236A (en) | 2019-05-30 |
| IL265236B1 IL265236B1 (en) | 2023-07-01 |
| IL265236B2 true IL265236B2 (en) | 2023-11-01 |
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| IL265236A IL265236B2 (en) | 2016-09-29 | 2017-09-27 | Multipurpose medical buildings and their uses |
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| EP (1) | EP3518953A4 (https=) |
| JP (1) | JP7133225B2 (https=) |
| CN (1) | CN109789183A (https=) |
| AU (2) | AU2017333442A1 (https=) |
| CA (1) | CA3037261A1 (https=) |
| IL (1) | IL265236B2 (https=) |
| WO (1) | WO2018061004A1 (https=) |
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| CN109789183A (zh) * | 2016-09-29 | 2019-05-21 | Aebi有限公司 | 治疗性多靶向构建体及其用途 |
| US20210198319A1 (en) * | 2017-09-27 | 2021-07-01 | Aebi Ltd. | Cytotoxic peptides and conjugates thereof |
| KR102268983B1 (ko) | 2019-09-11 | 2021-06-24 | 경북대학교 산학협력단 | 엔도테린 수용체 억제제에 의한 엑소좀 분비 억제 또는 pd-l1 발현 억제 용도 |
| CN112252362A (zh) * | 2020-10-10 | 2021-01-22 | 无锡市市政设施建设工程有限公司 | 基于bim实现地铁车站主体结构盘扣支架搭设的方法 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2010064207A2 (en) * | 2008-12-03 | 2010-06-10 | Koji Kawakami | Selective anticancer chimeric peptide |
| US20100151003A1 (en) * | 2006-12-21 | 2010-06-17 | Mohit Trikha | Egfr binding peptides and uses thereof |
| WO2013126690A1 (en) * | 2012-02-23 | 2013-08-29 | President And Fellows Of Harvard College | Modified microbial toxin receptor for delivering agents into cells |
| WO2015195721A1 (en) * | 2014-06-16 | 2015-12-23 | Purdue Research Foundation | Compositions and methods for treating cancer |
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|---|---|---|---|---|
| US20040058865A1 (en) | 2001-11-26 | 2004-03-25 | Danishefsky Samuel J | Homing peptide multimers, their preparation and uses |
| PT2949658T (pt) | 2003-03-03 | 2018-10-18 | Bracco Suisse Sa | Péptidos que ligam especificamente o recetor de hgf (cmet) e utilizações dos mesmos |
| WO2005090393A2 (en) | 2004-02-09 | 2005-09-29 | The Government Of The United States, As Represented By The Secretary Of Health And Human Services | Multimeric protein toxins to target cells having multiple identifying characteristics |
| US20090305898A1 (en) | 2005-07-21 | 2009-12-10 | Ilan Morad | Methods and Compositions for Identifying a Peptide Having an Intermolecular Interaction With a Target of Interest |
| US20100021473A1 (en) | 2005-12-06 | 2010-01-28 | Domantis Limited | Bispecific Ligands With Binding Specificity to Cell Surface Targets and Methods of Use Therefor |
| WO2007093373A2 (en) | 2006-02-14 | 2007-08-23 | Università Degli Studi Di Siena | Branched multimeric peptides for tumor diagnosis and therapy |
| US20080131428A1 (en) * | 2006-02-24 | 2008-06-05 | Arius Research, Inc. | Cytotoxicity mediation of cells evidencing surface expression of TROP-2 |
| PE20081140A1 (es) | 2006-10-25 | 2008-09-22 | Amgen Inc | Agentes terapeuticos a base de peptidos derivados de toxinas |
| CA2697922A1 (en) | 2007-08-28 | 2009-03-12 | Biogen Idec Ma Inc. | Compositions that bind multiple epitopes of igf-1r |
| CN102007145A (zh) | 2008-02-14 | 2011-04-06 | 百时美施贵宝公司 | 基于结合egfr的工程化蛋白质的靶向治疗剂 |
| EP2352522A4 (en) | 2008-11-06 | 2014-03-05 | Univ Washington | BISPECIFIC AUXILIARIES FOR INTRA-CELLULAR RELEASE |
| WO2010083495A2 (en) | 2009-01-18 | 2010-07-22 | The Board Of Trustees Of The Leland Stanford Junior University | Polypeptides targeting vascular endothelial growth factor receptor-2 and alpha v beta 3 integrin |
| WO2011047135A2 (en) | 2009-10-14 | 2011-04-21 | The Regents Of The University Of Colorado, A Body Corporate | Compositions and methods for treating bladder cancer |
| AU2011227714B2 (en) | 2010-03-19 | 2014-09-04 | Takeda Pharmaceutical Company Limited | TFPI inhibitors and methods of use |
| EP2714738B1 (en) * | 2011-05-24 | 2018-10-10 | Zyngenia, Inc. | Multivalent and monovalent multispecific complexes and their uses |
| CN110563850A (zh) * | 2012-04-30 | 2019-12-13 | 比奥孔有限公司 | 靶向/免疫调节性融合蛋白及其制造方法 |
| JP6103832B2 (ja) | 2012-06-25 | 2017-03-29 | Hoya株式会社 | Ｅｇｆｒ結合性ペプチド |
| CA3081073C (en) | 2013-03-12 | 2023-09-12 | Biocon Ltd. | Fusion immunomodulatory proteins and methods for making same |
| WO2015010094A1 (en) | 2013-07-18 | 2015-01-22 | Eutropics Pharmaceuticals, Inc. | Differential bh3 mitochondrial profiling |
| WO2015023979A1 (en) | 2013-08-16 | 2015-02-19 | Equip, Llc | Discrete peg constructs |
| CN109789183A (zh) * | 2016-09-29 | 2019-05-21 | Aebi有限公司 | 治疗性多靶向构建体及其用途 |
| US20210198319A1 (en) | 2017-09-27 | 2021-07-01 | Aebi Ltd. | Cytotoxic peptides and conjugates thereof |
| US20200339629A1 (en) | 2019-04-24 | 2020-10-29 | Aebi Ltd. | Therapeutic constructs comprising cmet binding peptides |
-
2017
- 2017-09-27 CN CN201780060289.8A patent/CN109789183A/zh active Pending
- 2017-09-27 EP EP17855166.9A patent/EP3518953A4/en active Pending
- 2017-09-27 CA CA3037261A patent/CA3037261A1/en active Pending
- 2017-09-27 US US16/337,163 patent/US11739163B2/en active Active
- 2017-09-27 IL IL265236A patent/IL265236B2/en unknown
- 2017-09-27 JP JP2019517069A patent/JP7133225B2/ja active Active
- 2017-09-27 WO PCT/IL2017/051094 patent/WO2018061004A1/en not_active Ceased
- 2017-09-27 AU AU2017333442A patent/AU2017333442A1/en not_active Abandoned
-
2022
- 2022-08-24 AU AU2022221434A patent/AU2022221434A1/en not_active Abandoned
-
2023
- 2023-07-06 US US18/348,229 patent/US20240002547A1/en active Pending
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20100151003A1 (en) * | 2006-12-21 | 2010-06-17 | Mohit Trikha | Egfr binding peptides and uses thereof |
| WO2010064207A2 (en) * | 2008-12-03 | 2010-06-10 | Koji Kawakami | Selective anticancer chimeric peptide |
| WO2013126690A1 (en) * | 2012-02-23 | 2013-08-29 | President And Fellows Of Harvard College | Modified microbial toxin receptor for delivering agents into cells |
| WO2015195721A1 (en) * | 2014-06-16 | 2015-12-23 | Purdue Research Foundation | Compositions and methods for treating cancer |
Non-Patent Citations (4)
| Title |
|---|
| CHANG, HAO-NAN, ET AL., BLOCKING OF THE PD?1/PD?L1 INTERACTION BY A D?PEPTIDE ANTAGONIST FOR CANCER IMMUNOTHERAPY. ANGEWANDTE CHEMIE INTERNATIONAL EDITION, 2015, 54.40: 11760-11764, 10 August 2015 (2015-08-10) * |
| KOHNO, MASAYUKI, ET AL., A NOVEL HYBRID PEPTIDE TARGETING EGFR-EXPRESSING CANCERS. EUROPEAN JOURNAL OF CANCER, 2011, 47.5: 773-783., 26 November 2010 (2010-11-26) * |
| MISHRA, PRAJNA; NAYAK, BISMITA; DEY, R. K., PEGYLATION IN ANTI-CANCER THERAPY: AN OVERVIEW. ASIAN JOURNAL OF PHARMACEUTICAL SCIENCES, 2016, 11.3: 337-348, 14 September 2015 (2015-09-14) * |
| WU, DONGDONG, ET AL., PEPTIDE-BASED CANCER THERAPY: OPPORTUNITY AND CHALLENGE. CANCER LETTERS, 2014, 351.1: 13-22, 13 May 2014 (2014-05-13) * |
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|---|---|
| US11739163B2 (en) | 2023-08-29 |
| CN109789183A (zh) | 2019-05-21 |
| IL265236A (en) | 2019-05-30 |
| US20240002547A1 (en) | 2024-01-04 |
| JP2020501513A (ja) | 2020-01-23 |
| US20190225711A1 (en) | 2019-07-25 |
| AU2017333442A1 (en) | 2019-04-04 |
| WO2018061004A1 (en) | 2018-04-05 |
| AU2022221434A1 (en) | 2022-10-06 |
| JP7133225B2 (ja) | 2022-09-08 |
| IL265236B1 (en) | 2023-07-01 |
| EP3518953A1 (en) | 2019-08-07 |
| CA3037261A1 (en) | 2018-04-05 |
| EP3518953A4 (en) | 2020-10-28 |
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