JP2009527498A5 - - Google Patents
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- JP2009527498A5 JP2009527498A5 JP2008555524A JP2008555524A JP2009527498A5 JP 2009527498 A5 JP2009527498 A5 JP 2009527498A5 JP 2008555524 A JP2008555524 A JP 2008555524A JP 2008555524 A JP2008555524 A JP 2008555524A JP 2009527498 A5 JP2009527498 A5 JP 2009527498A5
- Authority
- JP
- Japan
- Prior art keywords
- peptide
- seq
- capcna
- amino acid
- peptides
- Prior art date
- Legal status (The legal status 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 status listed.)
- Pending
Links
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 76
- 108050006400 Cyclin Proteins 0.000 claims description 23
- 102000009339 Proliferating Cell Nuclear Antigen Human genes 0.000 claims description 23
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 18
- 206010028980 Neoplasm Diseases 0.000 claims description 10
- 201000011510 cancer Diseases 0.000 claims description 9
- 239000000203 mixture Substances 0.000 claims description 8
- 102000004169 proteins and genes Human genes 0.000 claims description 6
- 108090000623 proteins and genes Proteins 0.000 claims description 6
- 102000001708 Protein Isoforms Human genes 0.000 claims description 5
- 108010029485 Protein Isoforms Proteins 0.000 claims description 5
- 230000002401 inhibitory effect Effects 0.000 claims description 5
- 230000003993 interaction Effects 0.000 claims description 5
- 230000004663 cell proliferation Effects 0.000 claims description 4
- 230000003211 malignant effect Effects 0.000 claims description 4
- 230000001225 therapeutic effect Effects 0.000 claims description 4
- 108010091748 peptide A Proteins 0.000 claims 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 24
- 210000004027 cell Anatomy 0.000 description 18
- 150000001413 amino acids Chemical class 0.000 description 12
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 12
- 102100031866 DNA excision repair protein ERCC-5 Human genes 0.000 description 6
- 239000003795 chemical substances by application Substances 0.000 description 5
- 238000003556 assay Methods 0.000 description 4
- 238000001727 in vivo Methods 0.000 description 4
- 108010032595 Antibody Binding Sites Proteins 0.000 description 3
- 239000002502 liposome Substances 0.000 description 3
- 230000035772 mutation Effects 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- 230000005945 translocation Effects 0.000 description 3
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 2
- 108090000672 Annexin A5 Proteins 0.000 description 2
- 102000004121 Annexin A5 Human genes 0.000 description 2
- AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- 101000766306 Homo sapiens Serotransferrin Proteins 0.000 description 2
- 102000003505 Myosin Human genes 0.000 description 2
- 108060008487 Myosin Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 102000007238 Transferrin Receptors Human genes 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 229920002521 macromolecule Polymers 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 238000000034 method Methods 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- XJMOSONTPMZWPB-UHFFFAOYSA-M propidium iodide Chemical compound [I-].[I-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 XJMOSONTPMZWPB-UHFFFAOYSA-M 0.000 description 2
- 230000004850 protein–protein interaction Effects 0.000 description 2
- XNSAINXGIQZQOO-SRVKXCTJSA-N protirelin Chemical compound NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H]1NC(=O)CC1)CC1=CN=CN1 XNSAINXGIQZQOO-SRVKXCTJSA-N 0.000 description 2
- 101800002011 Amphipathic peptide Proteins 0.000 description 1
- 108700031308 Antennapedia Homeodomain Proteins 0.000 description 1
- 101150019028 Antp gene Proteins 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 108010051109 Cell-Penetrating Peptides Proteins 0.000 description 1
- 102000020313 Cell-Penetrating Peptides Human genes 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 108010048671 Homeodomain Proteins Proteins 0.000 description 1
- 102000009331 Homeodomain Proteins Human genes 0.000 description 1
- 101001072338 Homo sapiens Proliferating cell nuclear antigen Proteins 0.000 description 1
- 102000003746 Insulin Receptor Human genes 0.000 description 1
- 108010001127 Insulin Receptor Proteins 0.000 description 1
- 108010088535 Pep-1 peptide Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 101710192266 Tegument protein VP22 Proteins 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 230000001640 apoptogenic effect Effects 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000008614 cellular interaction Effects 0.000 description 1
- 230000004700 cellular uptake Effects 0.000 description 1
- BHONFOAYRQZPKZ-LCLOTLQISA-N chembl269478 Chemical compound C([C@H](NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CCCNC(N)=N)[C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(O)=O)C1=CC=CC=C1 BHONFOAYRQZPKZ-LCLOTLQISA-N 0.000 description 1
- 229940044683 chemotherapy drug Drugs 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 229960004679 doxorubicin Drugs 0.000 description 1
- 238000009510 drug design Methods 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- -1 for example Proteins 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 102000044255 human PCNA Human genes 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000006662 intracellular pathway Effects 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 210000000214 mouth Anatomy 0.000 description 1
- 230000017074 necrotic cell death Effects 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 108010043655 penetratin Proteins 0.000 description 1
- MCYTYTUNNNZWOK-LCLOTLQISA-N penetratin Chemical compound C([C@H](NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CCCNC(N)=N)[C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(N)=O)C1=CC=CC=C1 MCYTYTUNNNZWOK-LCLOTLQISA-N 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 239000012679 serum free medium Substances 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 239000012096 transfection reagent Substances 0.000 description 1
- PBKWZFANFUTEPS-CWUSWOHSSA-N transportan Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(N)=O)[C@@H](C)CC)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)CN)[C@@H](C)O)C1=CC=C(O)C=C1 PBKWZFANFUTEPS-CWUSWOHSSA-N 0.000 description 1
- 108010062760 transportan Proteins 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US74331306P | 2006-02-17 | 2006-02-17 | |
| PCT/US2007/062335 WO2007098415A2 (en) | 2006-02-17 | 2007-02-16 | Peptide based inhibition of capcna protein-protein interactions in cancer |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2009527498A JP2009527498A (ja) | 2009-07-30 |
| JP2009527498A5 true JP2009527498A5 (enExample) | 2009-10-22 |
Family
ID=38235155
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2008555524A Pending JP2009527498A (ja) | 2006-02-17 | 2007-02-16 | 癌におけるｃａＰＣＮＡ相互作用のペプチドによる抑制 |
Country Status (9)
| Country | Link |
|---|---|
| US (3) | US8653039B2 (enExample) |
| EP (1) | EP1989225A2 (enExample) |
| JP (1) | JP2009527498A (enExample) |
| CN (1) | CN101384618A (enExample) |
| AU (1) | AU2007217037A1 (enExample) |
| BR (1) | BRPI0707948A2 (enExample) |
| CA (1) | CA2638866C (enExample) |
| EA (1) | EA200801847A1 (enExample) |
| WO (1) | WO2007098415A2 (enExample) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1989225A2 (en) * | 2006-02-17 | 2008-11-12 | Indiana University Research and Technology Corporation | Peptide based inhibition of capcna protein-protein interactions in cancer |
| WO2008036929A2 (en) * | 2006-09-21 | 2008-03-27 | Alnylam Pharmaceuticals, Inc. | Complex for transferring an anionic substance into a cell |
| GB0803352D0 (en) * | 2008-02-22 | 2008-04-02 | Ntnu Technology Transfer As | Oligopeptidic compounds and uses thereof |
| WO2010011890A2 (en) * | 2008-07-24 | 2010-01-28 | Indiana University Research And Technology Corporation | Cancer peptide therapeutics |
| FR2942798B1 (fr) * | 2009-03-05 | 2011-04-08 | Centre Nat Rech Scient | Peptides utilisables pour le traitement de la leucemie lymphoide chronique |
| US20120195978A1 (en) * | 2009-10-07 | 2012-08-02 | Indiana University Research And Technology Corpora | Capcna peptide therapeutics for cancer |
| EP2538959A1 (en) * | 2010-02-24 | 2013-01-02 | Institut National de la Santé et de la Recherche Médicale | Compounds for the treatment of inflammation and neutropenia |
| WO2011113942A2 (en) * | 2010-03-18 | 2011-09-22 | Institut National De La Sante Et De La Recherche Medicale (Inserm) | Method for predicting the responsiveness to chemotherapy |
| EP2819700B1 (en) | 2012-02-27 | 2016-12-21 | Universitat de Barcelona | Protease-resistant compounds useful as shuttles through the blood-brain barrier and shuttle-cargo constructs |
| GB201214007D0 (en) * | 2012-08-07 | 2012-09-19 | Scancell Ltd | Anti-tumour immune responses to modified self-epitopes |
| US10420840B2 (en) * | 2015-04-10 | 2019-09-24 | Rll, Llc | Anticancer therapeutic agents |
| IL267340B2 (en) * | 2016-12-15 | 2023-12-01 | Nat Inst Biotechnology Negev Ltd | Monoclonal antibodies against PCNA and their use |
| GB201815041D0 (en) | 2018-09-14 | 2018-10-31 | Scancell Ltd | Epitopes |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5935797A (en) * | 1994-06-16 | 1999-08-10 | Stanford University | Interaction of MHC Class II proteins with members of the PCNA family of proteins |
| GB9509557D0 (en) * | 1995-05-11 | 1995-07-05 | Univ Dundee | PCNA binding substance |
| WO1999065515A2 (en) * | 1998-06-15 | 1999-12-23 | Arch Development Corporation | Combination of radiotherapy and anti-angiogenic factors |
| US7294471B2 (en) | 2002-02-27 | 2007-11-13 | Cskeys, Llc | Method for purifying cancer-specific proliferating cell nuclear antigen |
| WO2006116631A2 (en) * | 2005-04-27 | 2006-11-02 | Indiana University Research And Technology Corporation | Cancer specific pcna isoform binding antibodies and uses thereof |
| AU2006261856B2 (en) * | 2005-06-27 | 2012-07-05 | Indiana University Research And Technology Corporation | csPCNA isoform modifications and uses thereof |
| EP1989225A2 (en) * | 2006-02-17 | 2008-11-12 | Indiana University Research and Technology Corporation | Peptide based inhibition of capcna protein-protein interactions in cancer |
-
2007
- 2007-02-16 EP EP07757135A patent/EP1989225A2/en not_active Withdrawn
- 2007-02-16 EA EA200801847A patent/EA200801847A1/ru unknown
- 2007-02-16 CA CA2638866A patent/CA2638866C/en active Active
- 2007-02-16 AU AU2007217037A patent/AU2007217037A1/en not_active Abandoned
- 2007-02-16 CN CNA2007800052894A patent/CN101384618A/zh active Pending
- 2007-02-16 WO PCT/US2007/062335 patent/WO2007098415A2/en not_active Ceased
- 2007-02-16 BR BRPI0707948-6A patent/BRPI0707948A2/pt not_active Application Discontinuation
- 2007-02-16 JP JP2008555524A patent/JP2009527498A/ja active Pending
- 2007-02-16 US US12/279,028 patent/US8653039B2/en active Active
-
2014
- 2014-02-18 US US14/182,550 patent/US9187526B2/en active Active
-
2015
- 2015-10-29 US US14/926,904 patent/US20160304559A1/en not_active Abandoned
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