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  1. Article ; Online: p28-Mediated Activation of p53 in G2-M Phase of the Cell Cycle Enhances the Efficacy of DNA Damaging and Antimitotic Chemotherapy.

    Yamada, Tohru / Das Gupta, Tapas K / Beattie, Craig W

    Cancer research

    2016  Volume 76, Issue 8, Page(s) 2354–2365

    Abstract: p28 is an anionic cell-penetrating peptide of 28 amino acids that activates wild-type and mutated p53, leading subsequently to selective inhibition of CDK2 and cyclin A expression and G2-M cell-cycle arrest. In this study, we investigated the cytotoxic ... ...

    Abstract p28 is an anionic cell-penetrating peptide of 28 amino acids that activates wild-type and mutated p53, leading subsequently to selective inhibition of CDK2 and cyclin A expression and G2-M cell-cycle arrest. In this study, we investigated the cytotoxic effects of p28 treatment alone and in combination with DNA-damaging and antimitotic agents on human cancer cells. p28 enhanced the cytotoxic activity of lower concentrations (IC20-50) of DNA-damaging drugs (doxorubicin, dacarbazine, temozolamide) or antimitotic drugs (paclitaxel and docetaxel) in a variety of cancer cells expressing wild-type or mutated p53. Mechanistic investigations revealed that p28 induced a post-translational increase in the expression of wild-type or mutant p53 and p21, resulting in cell-cycle inhibition at the G2-M phase. The enhanced activity of these anticancer agents in combination with p28 was facilitated through the p53/p21/CDK2 pathway. Taken together, these results highlight a new approach to maximize the efficacy of chemotherapeutic agents while reducing dose-related toxicity. Cancer Res; 76(8); 2354-65. ©2016 AACR.
    MeSH term(s) Amino Acid Sequence ; Animals ; Antineoplastic Agents/pharmacology ; Cell Division ; Cell Line, Tumor ; Cell-Penetrating Peptides/chemistry ; Cell-Penetrating Peptides/physiology ; DNA Damage ; Dacarbazine/analogs & derivatives ; Dacarbazine/pharmacology ; Female ; G2 Phase ; Heterografts ; Male ; Mice, Nude ; Tumor Suppressor Protein p53/metabolism
    Chemical Substances Antineoplastic Agents ; Cell-Penetrating Peptides ; TP53 protein, human ; Tumor Suppressor Protein p53 ; Dacarbazine (7GR28W0FJI) ; temozolomide (YF1K15M17Y)
    Language English
    Publishing date 2016--15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1432-1
    ISSN 1538-7445 ; 0008-5472
    ISSN (online) 1538-7445
    ISSN 0008-5472
    DOI 10.1158/0008-5472.CAN-15-2355
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  2. Article ; Online: British Society of Haematology Guidelines on the spectrum of fresh frozen plasma and cryoprecipitate products: their handling and use in various patient groups in the absence of major bleeding (Br J Haematol. 2018;181:54-67). Addendum August 2020.

    Green, Laura / Bolton-Maggs, Paula / Beattie, Craig / Cardigan, Rebecca / Kallis, Yiannis / Stanworth, Simon J / Thachil, Jecko / Zahra, Sharon

    British journal of haematology

    2020  Volume 191, Issue 5, Page(s) 728–729

    MeSH term(s) Hematologic Agents ; Hematology ; Hemorrhage/etiology ; Humans ; Plasma
    Chemical Substances Hematologic Agents
    Language English
    Publishing date 2020-11-18
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 80077-6
    ISSN 1365-2141 ; 0007-1048
    ISSN (online) 1365-2141
    ISSN 0007-1048
    DOI 10.1111/bjh.17104
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  3. Article ; Online: p28, an anionic cell-penetrating peptide, increases the activity of wild type and mutated p53 without altering its conformation.

    Yamada, Tohru / Das Gupta, Tapas K / Beattie, Craig W

    Molecular pharmaceutics

    2013  Volume 10, Issue 9, Page(s) 3375–3383

    Abstract: p28, a cell penetrating peptide, binds to the DNA binding domain (DBD) of p53, inducing a post-translational increase in intracellular levels of wild type and mutant p53 activating pathways that inhibit cancer cell proliferation at G2/M. Cancer cells ... ...

    Abstract p28, a cell penetrating peptide, binds to the DNA binding domain (DBD) of p53, inducing a post-translational increase in intracellular levels of wild type and mutant p53 activating pathways that inhibit cancer cell proliferation at G2/M. Cancer cells respond to p28 with an increase in p53 activity, except when mutations either alter DNA contact or completely unfold the DBD. The increase in p53 activity is accompanied by a significant reduction in the level of the E3 ligase COP1, with no alteration in p53 conformation. This suggests p28 can activate p53 over a wide range of conformational mutations by inhibiting the binding of COP1 to p53.
    MeSH term(s) Cell Line ; Cell Line, Tumor ; Cell-Penetrating Peptides/pharmacology ; Humans ; Molecular Dynamics Simulation ; Mutation ; Protein Binding ; Protein Conformation/drug effects ; Reverse Transcriptase Polymerase Chain Reaction ; Tumor Suppressor Protein p53/chemistry ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Ubiquitin-Protein Ligases/chemistry ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances Cell-Penetrating Peptides ; Tumor Suppressor Protein p53 ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2013-09-03
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2138405-8
    ISSN 1543-8392 ; 1543-8384
    ISSN (online) 1543-8392
    ISSN 1543-8384
    DOI 10.1021/mp400221r
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  4. Article: Binding of Amphipathic Cell Penetrating Peptide p28 to Wild Type and Mutated p53 as studied by Raman, Atomic Force and Surface Plasmon Resonance spectroscopies.

    Signorelli, Sara / Santini, Simona / Yamada, Tohru / Bizzarri, Anna Rita / Beattie, Craig W / Cannistraro, Salvatore

    Biochimica et biophysica acta. General subjects

    2017  Volume 1861, Issue 4, Page(s) 910–921

    Abstract: Background: Mutations within the DNA binding domain (DBD) of the tumor suppressor p53 are found in >50% of human cancers and may significantly modify p53 secondary structure impairing its function. p28, an amphipathic cell-penetrating peptide, binds to ... ...

    Abstract Background: Mutations within the DNA binding domain (DBD) of the tumor suppressor p53 are found in >50% of human cancers and may significantly modify p53 secondary structure impairing its function. p28, an amphipathic cell-penetrating peptide, binds to the DBD through hydrophobic interaction and induces a posttranslational increase in wildtype and mutant p53 restoring functionality. We use mutation analyses to explore which elements of secondary structure may be critical to p28 binding.
    Methods: Molecular modeling, Raman spectroscopy, Atomic Force Spectroscopy (AFS) and Surface Plasmon Resonance (SPR) were used to identify which secondary structure of site-directed and naturally occurring mutant DBDs are potentially altered by discrete changes in hydrophobicity and the molecular interaction with p28.
    Results: We show that specific point mutations that alter hydrophobicity within non-mutable and mutable regions of the p53 DBD alter specific secondary structures. The affinity of p28 was positively correlated with the β-sheet content of a mutant DBD, and reduced by an increase in unstructured or random coil that resulted from a loss in hydrophobicity and redistribution of surface charge.
    Conclusions: These results help refine our knowledge of how mutations within p53-DBD alter secondary structure and provide insight on how potential structural alterations in p28 or similar molecules improve their ability to restore p53 function.
    General significance: Raman spectroscopy, AFS, SPR and computational modeling are useful approaches to characterize how mutations within the p53DBD potentially affect secondary structure and identify those structural elements prone to influence the binding affinity of agents designed to increase the functionality of p53.
    MeSH term(s) Amino Acid Sequence ; Binding Sites/genetics ; Cell Line, Tumor ; Cell-Penetrating Peptides/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Microscopy, Atomic Force/methods ; Models, Molecular ; Molecular Dynamics Simulation ; Mutation/genetics ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Protein Binding/genetics ; Protein Structure, Secondary ; Surface Plasmon Resonance/methods ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism
    Chemical Substances Cell-Penetrating Peptides ; DNA-Binding Proteins ; Peptide Fragments ; Tumor Suppressor Protein p53
    Language English
    Publishing date 2017-01-24
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0304-4165 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0304-4165 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbagen.2017.01.022
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  5. Article ; Online: British Society of Haematology Guidelines on the spectrum of fresh frozen plasma and cryoprecipitate products: their handling and use in various patient groups in the absence of major bleeding.

    Green, Laura / Bolton-Maggs, Paula / Beattie, Craig / Cardigan, Rebecca / Kallis, Yiannis / Stanworth, Simon J / Thachil, Jecko / Zahra, Sharon

    British journal of haematology

    2018  Volume 181, Issue 1, Page(s) 54–67

    MeSH term(s) Blood Component Transfusion ; Factor VIII/therapeutic use ; Fibrinogen/therapeutic use ; Hematology ; Hemorrhage/prevention & control ; Humans ; Plasma ; Societies, Medical ; United Kingdom
    Chemical Substances cryoprecipitate coagulum ; Factor VIII (9001-27-8) ; Fibrinogen (9001-32-5)
    Language English
    Publishing date 2018-03-12
    Publishing country England
    Document type Letter ; Systematic Review
    ZDB-ID 80077-6
    ISSN 1365-2141 ; 0007-1048
    ISSN (online) 1365-2141
    ISSN 0007-1048
    DOI 10.1111/bjh.15167
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  6. Article ; Online: Chirality switching within an anionic cell-penetrating peptide inhibits translocation without affecting preferential entry.

    Yamada, Tohru / Signorelli, Sara / Cannistraro, Salvatore / Beattie, Craig W / Bizzarri, Anna Rita

    Molecular pharmaceutics

    2015  Volume 12, Issue 1, Page(s) 140–149

    Abstract: Multiple substitution of d- for l-amino acids decreases the intracellular uptake of cationic cell penetrating peptides (CPP) in a cell line-dependent manner. We show here that a single d-amino acid substitution can decrease the overall uptake of the ... ...

    Abstract Multiple substitution of d- for l-amino acids decreases the intracellular uptake of cationic cell penetrating peptides (CPP) in a cell line-dependent manner. We show here that a single d-amino acid substitution can decrease the overall uptake of the anionic, amphipathic CPP, p28, into cancer and histologically matched normal cell lines, while not altering the preferential uptake of p28 into cancer cells. The decrease appears dependent on the position of the d-substitution within the peptide and the ability of the substituted d-amino acid to alter chirality. We also suggest that when d-substitution alters the ratio of α-helix to β-sheet content of an anionic CPP, its translocation across the cell membrane is altered, reducing overall entry. These observations may have a significant effect on the design of future d-substituted analogues of cell penetrating peptides.
    MeSH term(s) Amino Acid Substitution ; Amino Acids/chemistry ; Anions ; Antineoplastic Agents/chemistry ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cell Separation ; Cell-Penetrating Peptides/chemistry ; Circular Dichroism ; Flow Cytometry ; Hep G2 Cells ; Humans ; MCF-7 Cells ; Protein Structure, Secondary ; Spectrum Analysis, Raman ; Stereoisomerism
    Chemical Substances Amino Acids ; Anions ; Antineoplastic Agents ; Cell-Penetrating Peptides
    Language English
    Publishing date 2015-01-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2138405-8
    ISSN 1543-8392 ; 1543-8384
    ISSN (online) 1543-8392
    ISSN 1543-8384
    DOI 10.1021/mp500495u
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  7. Article ; Online: Addendum to the British Committee for Standards in Haematology (BCSH): Guidelines for the use of fresh-frozen plasma, cryoprecipitate and cryosupernatant, 2004 (Br. J Haematol 2004,126,11-28).

    Green, Laura / Cardigan, Rebecca / Beattie, Craig / Bolton-Maggs, Paula / Stanworth, Simon J / Thachil, Jecko / Kallis, Yiannis / Zahra, Sharon

    British journal of haematology

    2017  Volume 178, Issue 4, Page(s) 646–647

    Language English
    Publishing date 2017-08
    Publishing country England
    Document type Letter
    ZDB-ID 80077-6
    ISSN 1365-2141 ; 0007-1048
    ISSN (online) 1365-2141
    ISSN 0007-1048
    DOI 10.1111/bjh.14163
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  8. Article ; Online: A nanotechnological, molecular-modeling, and immunological approach to study the interaction of the anti-tumorigenic peptide p28 with the p53 family of proteins.

    Coppari, Emilia / Yamada, Tohru / Bizzarri, Anna Rita / Beattie, Craig W / Cannistraro, Salvatore

    International journal of nanomedicine

    2014  Volume 9, Page(s) 1799–1813

    Abstract: p28 is an anionic, amphipathic, cell-penetrating peptide derived from the cupredoxin azurin that binds to the DNA-binding domain (DBD) of the tumor suppressor protein, p53, and induces a post-translational increase in the level of wild type and mutated ... ...

    Abstract p28 is an anionic, amphipathic, cell-penetrating peptide derived from the cupredoxin azurin that binds to the DNA-binding domain (DBD) of the tumor suppressor protein, p53, and induces a post-translational increase in the level of wild type and mutated p53 in a wide variety of human cancer cells. As p63 and p73, additional members of the p53 superfamily of proteins, also appear to be involved in the cellular response to cancer therapy and are reportedly required for p53-induced apoptosis, we asked whether p28 also binds to p63 and p73. Atomic force spectroscopy demonstrates that p28 forms a stable, high-affinity complex with full-length p63, the DBD of p63, and full-length p73. Exposure to p28 decreased the level of TAp63α and ΔNp63α, the truncated form of p63, in p53 wild type and mutated human breast cancer cells, respectively. p28 increased the level of TAp73α, but not ΔNp73α, in the same breast cancer cell lines. In contrast, p28 increased the level of the TA and ΔN isoforms of p63 in p53 wild type, but not in p53 mutated melanoma cells, while decreasing TA p73α in p53 wild type and mutated human melanoma cells. All changes were mirrored by an associated change in the expression of the HECT E3 ligases Itch/AIP4, AIP5, and the RING E3 ligase Pirh2, but not in the receptor for activated C kinase or the RING E3 ligases Mdm2 and Cop1. Collectively, the data suggest that molecules such as p28 bind with high affinity to the DBD of p63 and p73 and alter their expression independent of the Mdm2 and Cop1 pathways.
    MeSH term(s) Antineoplastic Agents/immunology ; Azurin/chemistry ; Azurin/immunology ; Azurin/ultrastructure ; Binding Sites ; Cell Line, Tumor ; Computer Simulation ; Humans ; Models, Chemical ; Models, Immunological ; Models, Molecular ; Neoplasms, Experimental/chemistry ; Neoplasms, Experimental/immunology ; Peptide Fragments/chemistry ; Peptide Fragments/immunology ; Peptide Fragments/ultrastructure ; Protein Binding ; Protein Interaction Mapping ; Tumor Suppressor Protein p53/chemistry ; Tumor Suppressor Protein p53/metabolism ; Tumor Suppressor Protein p53/ultrastructure
    Chemical Substances Antineoplastic Agents ; Peptide Fragments ; Tumor Suppressor Protein p53 ; Azurin (12284-43-4) ; azurin (50-77) (H4QZU9L323)
    Language English
    Publishing date 2014-04-10
    Publishing country New Zealand
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2364941-0
    ISSN 1178-2013 ; 1176-9114
    ISSN (online) 1178-2013
    ISSN 1176-9114
    DOI 10.2147/IJN.S58465
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  9. Article ; Online: Binding of azurin to cytochrome c 551 as investigated by surface plasmon resonance and fluorescence.

    Santini, Simona / Bizzarri, Anna Rita / Yamada, Tohru / Beattie, Craig W / Cannistraro, Salvatore

    Journal of molecular recognition : JMR

    2014  Volume 27, Issue 3, Page(s) 124–130

    Abstract: The interaction between azurin (Az) and cytochrome c 551 (CytC551) from Pseudomonas aeruginosa deserves particular interest for both its physiological aspects and their possible applications in bionano devices. Here, the kinetics of the interaction has ... ...

    Abstract The interaction between azurin (Az) and cytochrome c 551 (CytC551) from Pseudomonas aeruginosa deserves particular interest for both its physiological aspects and their possible applications in bionano devices. Here, the kinetics of the interaction has been studied by surface plasmon resonance and fluorescence quenching. Surface plasmon resonance data have been successfully interpreted by the heterogeneous ligand model, which predicts the existence of two binding sites on the immobilized Az for CytC551 molecules in solution. On the other hand, the fluorescence study indicates the formation of a complex, with the involvement of the lone Az tryptophan (Trp) at position 48. The two different techniques point out the occurrence of an encounter complex between Az and CytC551 that evolves toward the formation of a more stable complex characterized by an equilibrium dissociation constant KD typical of transient interactions.
    MeSH term(s) Azurin/chemistry ; Azurin/genetics ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Binding Sites ; Cytochrome c Group/chemistry ; Cytochrome c Group/genetics ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Kinetics ; Models, Molecular ; Protein Binding ; Pseudomonas aeruginosa/chemistry ; Pseudomonas aeruginosa/genetics ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Spectrometry, Fluorescence ; Surface Plasmon Resonance ; Thermodynamics
    Chemical Substances Bacterial Proteins ; Cytochrome c Group ; Recombinant Proteins ; Azurin (12284-43-4) ; cytochrome C(551) (9048-77-5)
    Language English
    Publishing date 2014-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1015084-5
    ISSN 1099-1352 ; 0952-3499
    ISSN (online) 1099-1352
    ISSN 0952-3499
    DOI 10.1002/jmr.2346
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  10. Article ; Online: Addendum to the British Committee for Standards in Haematology (BCSH): guidelines for the use of fresh-frozen plasma, cryoprecipitate and cryosupernatant, 2004 (Br. J Haematol 2004,126,11-28) - response to Neisser-Svae and Heger.

    Green, Laura / Cardigan, Rebecca / Beattie, Craig / Bolton-Maggs, Paula / Stanworth, Simon J / Thachil, Jecko / Kallis, Yiannis / Zahra, Sharon

    British journal of haematology

    2016  Volume 180, Issue 5, Page(s) 749–750

    MeSH term(s) Hematologic Agents ; Hematology ; Plasma ; Reference Standards
    Chemical Substances Hematologic Agents
    Language English
    Publishing date 2016-11-23
    Publishing country England
    Document type Letter ; Comment
    ZDB-ID 80077-6
    ISSN 1365-2141 ; 0007-1048
    ISSN (online) 1365-2141
    ISSN 0007-1048
    DOI 10.1111/bjh.14434
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