Relevant bibliographies by topics / Peptide Prodrugs

Academic literature on the topic 'Peptide Prodrugs'

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Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Peptide Prodrugs"

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Zhang, Richard, and Haishan Lin. "Abstract 5204: Optimization of novel anti-human CD47 antibody prodrugs as cancer therapeutics with low on-target toxicity." Cancer Research 82, no. 12_Supplement (June 15, 2022): 5204. http://dx.doi.org/10.1158/1538-7445.am2022-5204.

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Abstract CD47 is a well-studied target for cancer immunotherapy. Blocking of CD47 binding to its receptor, SIRPα, on macrophages leads to inhibition of macrophage activation and phagocytosis. Several monoclonal anti-CD47 antibodies are currently in various stages of clinical development. However, since CD47 is also expressed on normal cells such as red blood cells and platelets, anti-CD47 antibodies also caused on-target side effects during clinical evaluations, such as anemia and red blood cell hemagglutination. To minimize the on-target side effects of anti-CD47 antibodies, we have generated anti-CD47 prodrugs. By screening a phage peptide library, we identified peptides that can specifically block the anti-CD47 antibody binding activity. These peptides were fused to the humanized anti-CD47 antibody via a linker containing protease substrate sequences to derive the anti-CD47 antibody prodrug. We demonstrated that these anti-CD47 antibody prodrugs had significantly diminished CD47 binding activity and were unable to block CD47:SIRPα interaction. Upon cleavage of the anti-CD47 antibody prodrug with proteases, the antibody regained full activities in both binding to CD47 and blocking CD47:SIRPα interaction. Importantly, we showed that the anti-CD47 antibody prodrug had minimal hemagglutination and RBC binding activities. Since different tumors may have different types of protease activities, anti-CD47 prodrugs with different types of protease substrates have been generated to demonstrate that the anti-CD47 prodrug can be used for treating various tumor types. These data suggest that novel anti-CD47 antibody prodrugs are promising candidates for the next generation anti-CD47 therapeutics with improved safety profile. Citation Format: Richard Zhang, Haishan Lin. Optimization of novel anti-human CD47 antibody prodrugs as cancer therapeutics with low on-target toxicity [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 5204.
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THOMAS, W. A. "Peptide derivatives as prodrugs." Biochemical Society Transactions 14, no. 2 (April 1, 1986): 383–87. http://dx.doi.org/10.1042/bst0140383.

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McKenna, Charles E., Boris A. Kashemirov, Ulrika Eriksson, Gordon L. Amidon, Phillip E. Kish, Stefanie Mitchell, Jae-Seung Kim, and John M. Hilfinger. "Cidofovir peptide conjugates as prodrugs." Journal of Organometallic Chemistry 690, no. 10 (May 2005): 2673–78. http://dx.doi.org/10.1016/j.jorganchem.2005.03.004.

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Janssen, Samuel, Carsten M. Jakobsen, D. Marc Rosen, Rebecca M. Ricklis, Ulrich Reineke, Soeren B. Christensen, Hans Lilja, and Samuel R. Denmeade. "Screening a combinatorial peptide library to develop a human glandular kallikrein 2–activated prodrug as targeted therapy for prostate cancer." Molecular Cancer Therapeutics 3, no. 11 (November 1, 2004): 1439–50. http://dx.doi.org/10.1158/1535-7163.1439.3.11.

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Abstract Objective: Prostate cancer cells secrete the unique protease human glandular kallikrein 2 (hK2) that represents a target for proteolytic activation of cytotoxic prodrugs. The objective of this study was to identify hK2-selective peptide substrates that could be coupled to a cytotoxic analogue of thapsigargin, a potent inhibitor of the sarcoplasmic/endoplasmic reticulum calcium ATPase pump that induces cell proliferation–independent apoptosis through dysregulation of intracellular calcium levels. Methods: To identify peptide sequence requirements for hK2, a combination of membrane-bound peptides (SPOT analysis) and combinatorial chemistry using fluorescence-quenched peptide substrates was used. Peptide substrates were then coupled to 8-O-(12[l-leucinoylamino]dodecanoyl)-8-O-debutanoylthapsigargin (L12ADT), a potent analogue of thapsigargin, to produce a prodrug that was then characterized for hK2 hydrolysis, plasma stability, and in vitro cytotoxicity. Results: Both techniques indicated that a peptide with two arginines NH2-terminal of the scissile bond produced the highest rates of hydrolysis. A lead peptide substrate with the sequence Gly-Lys-Ala-Phe-Arg-Arg (GKAFRR) was hydrolyzed by hK2 with a Km of 26.5 μmol/L, kcat of 1.09 s−1, and a kcat/Km ratio of 41,132 s−1 mol/L−1. The GKAFRR-L12ADT prodrug was rapidly hydrolyzed by hK2 and was stable in plasma, whereas the GKAFRR-L peptide substrate was unstable in human plasma. The hK2-activated thapsigargin prodrug was not activated by cathepsin B, cathepsin D, and urokinase but was an excellent substrate for plasmin. The GKAFRR-L12ADT was selectively cytotoxic in vitro to cancer cells in the presence of enzymatically active hK2. Conclusion: The hK2-activated thapsigargin prodrug represents potential novel targeted therapy for prostate cancer.
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Forde, Éanna, Hilary Humphreys, Catherine M. Greene, Deirdre Fitzgerald-Hughes, and Marc Devocelle. "Potential of Host Defense Peptide Prodrugs as Neutrophil Elastase-Dependent Anti-Infective Agents for Cystic Fibrosis." Antimicrobial Agents and Chemotherapy 58, no. 2 (November 25, 2013): 978–85. http://dx.doi.org/10.1128/aac.01167-13.

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ABSTRACTHost defense peptides (HDPs) are short antimicrobial peptides of the innate immune system. Deficiencies in HDPs contribute to enhanced susceptibility to infections, e.g., in cystic fibrosis (CF). Exogenous HDPs can compensate for these deficiencies, but their development as antimicrobials is limited by cytotoxicity. Three HDP prodrugs were designed so their net positive charge is masked by a promoiety containing a substrate for the enzyme neutrophil elastase (NE). This approach can confine activation to sites with high NE levels. Enzyme-labile peptides were synthesized, and their activation was investigated using purified NE. Susceptibilities ofPseudomonas aeruginosato parent and prodrug peptides in the presence and absence of NE-rich CF human bronchoalveolar lavage (BAL) fluid and different NaCl concentrations were compared. The effect of the HDP promoiety on cytotoxicity was determined with cystic fibrosis bronchial epithelial (CFBE41o-) cells. NE in CF BAL fluids activated the HDP prodrugs, restoring bactericidal activity against reference and clinical isolates ofP. aeruginosa. However, activation also required the addition of 300 mM NaCl. Under these conditions, the bactericidal activity levels of the HDP prodrugs differed, with pro-P18 demonstrating the greatest activity (90% to 100% of that of the parent, P18, at 6.25 μg/ml). Cytotoxic effects on CFBE41o- cells were reduced by the addition of the promoiety to HDPs. We demonstrate here for the first time the selective activation of novel HDP prodrugs by a host disease-associated enzyme atin vivoconcentrations of the CF lung. This approach may lead to the development of novel therapeutic agents with low toxicity that are active under the challenging conditions of the CF lung.
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Forde, Eanna, and Marc Devocelle. "Pro-Moieties of Antimicrobial Peptide Prodrugs." Molecules 20, no. 1 (January 13, 2015): 1210–27. http://dx.doi.org/10.3390/molecules20011210.

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Forde, Éanna, André Schütte, Emer Reeves, Catherine Greene, Hilary Humphreys, Marcus Mall, Deirdre Fitzgerald-Hughes, and Marc Devocelle. "DifferentialIn VitroandIn VivoToxicities of Antimicrobial Peptide Prodrugs for Potential Use in Cystic Fibrosis." Antimicrobial Agents and Chemotherapy 60, no. 5 (February 22, 2016): 2813–21. http://dx.doi.org/10.1128/aac.00157-16.

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ABSTRACTThere has been considerable interest in the use of antimicrobial peptides (AMPs) as antimicrobial agents for the treatment of many conditions, including cystic fibrosis (CF). The challenging conditions of the CF patient lung require robust AMPs that are active in an environment of high proteolytic activity but that also have low cytotoxicity and immunogenicity. Previously, we developed prodrugs of AMPs that limited the cytotoxic effects of AMP treatment by rendering the antimicrobial activity dependent on the host enzyme neutrophil elastase (NE). However, cytotoxicity remained an issue. Here, we describe the further optimization of the AMP prodrug (pro-AMP) model for CF to produce pro-WMR, a peptide with greatly reduced cytotoxicity (50% inhibitory concentration against CFBE41o- cells, >300 μM) compared to that of the previous group of pro-AMPs. The bactericidal activity of pro-WMR was increased in NE-rich bronchoalveolar lavage (BAL) fluid from CF patients (range, 8.4% ± 6.9% alone to 91.5% ± 5.8% with BAL fluid;P= 0.0004), an activity differential greater than that of previous pro-AMPs. In a murine model of lung delivery, the pro-AMP modification reduced host toxicity, with pro-WMR being less toxic than the active peptide. Previously, host toxicity issues have hampered the clinical application of AMPs. However, the development of application-specific AMPs with modifications that minimize toxicity similar to those described here can significantly advance their potential use in patients. The combination of this prodrug strategy with a highly active AMP has the potential to produce new therapeutics for the challenging conditions of the CF patient lung.
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Wei, Yaoming, and Dehua Pei. "Activation of antibacterial prodrugs by peptide deformylase." Bioorganic & Medicinal Chemistry Letters 10, no. 10 (May 2000): 1073–76. http://dx.doi.org/10.1016/s0960-894x(00)00167-0.

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Lee, Jiyoun, Wei Huang, James M. Broering, Annelise E. Barron, and Jiwon Seo. "Prostate tumor specific peptide–peptoid hybrid prodrugs." Bioorganic & Medicinal Chemistry Letters 25, no. 14 (July 2015): 2849–52. http://dx.doi.org/10.1016/j.bmcl.2015.04.092.

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Freeman, Hanna, Selvi Srinivasan, Debobrato Das, Patrick S. Stayton, and Anthony J. Convertine. "Fully synthetic macromolecular prodrug chemotherapeutics with EGFR targeting and controlled camptothecin release kinetics." Polymer Chemistry 9, no. 42 (2018): 5224–33. http://dx.doi.org/10.1039/c8py01047a.

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Dissertations / Theses on the topic "Peptide Prodrugs"

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Potok, Stephanie. "Peptide rotaxanes as potential prodrugs." Thesis, University of Edinburgh, 2004. http://hdl.handle.net/1842/12131.

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Peptides are potential therapeutic agents involved in a wide range of biological processes. In principle, rotaxanes can be used as novel prodrug delivery systems to overcome the problems of peptide degradation in vivo and their poor membrane transport permeability. The presence of the macrocycle around the peptide thread acts as a protective shield against peptidases and modifies its cell membrane transport characteristics. However, the classical ‘clipping’ method of rotaxane formation is mainly limited to dipeptide sequences since the presence of intramolecular hydrogen bonds in longer threads causes folding of the backbone, preventing good interactions with the precursor to the macrocycle. This thesis focused on the synthesis of short peptide rotaxane building blocks. Their elongation on both sides of the peptide backbone was then applied to the straightforward synthesis of oligopeptide [2] and [3]rotaxanes in very good yields.
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Fernandes, Anthony. "Synthetic molecular nanodevices for selective peptide-based therapy." Thesis, University of Edinburgh, 2009. http://hdl.handle.net/1842/4037.

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During this thesis we tried to design, synthesise and analyse some novel devices for the selective delivery of peptides. These systems are based on the enzyme-activated anticancer prodrugs developed by Prof. Gesson in Poitiers and the peptide rotaxanes developed by Prof. Leigh in Edinburgh. The innovative rotaxanes we constructed are devised to protect and selectively release a peptide in response to an enzyme-specific stimulus for the targeted therapy of cancer. In Chapter 1 we tried to expose the main synthetic strategies aimed at improving the stability and permeation features of biologically active peptides. We examined some prodrug approaches and particularly the tumour-activated prodrugs (TAPs), largely investigated for use in anticancer chemotherapy. TAPs are generally three-part molecules composed of trigger, spacer and effector units. We also presented the original methodology developed by Prof. Leigh, namely the hydrogen bond-directed assembly of peptide rotaxanes, to protect a peptide thread from external environment. Finally we presented our project which consists of a combination of the peptide prodrug and rotaxane approaches. Therefore, based on the knowledge of both research groups we tried in Chapter 2 to develop some model systems in order to study the influence of the rotaxane architecture upon prodrug molecules. The first step towards such rotaxane-based peptide prodrugs relied on the efficient design of a spacer which has to be bulky enough to work as a stopper for the macrocycle. Much of the work presented in this chapter is based on the design and synthesis of such self-immolative units. We then explored the response of our model rotaxanes under the action of the activating enzyme. After this detailed study, in Chapter 3 we applied our concept to the biologically active peptide Met-enkephalin. In this chapter we presented a comparison between a rotaxane prodrug of Met-enkephalin and its non-interlocked derivative. Thus both compounds were successfully synthesised and evaluated to release the free peptide after enzymatic activation. The protective effect of encapsulating the peptide within a rotaxane assembly was also studied in human plasma and with different proteases. Finally, in Chapter 4, we introduced the construction of a rotaxane-based molecular machine programmed to synthesise a short peptide unit from the amino acids carried on its thread. We synthesised with success a one-station model rotaxane to study the catalyst effect of the macrocycle. Unfortunately this model machine proved not to work and current research is still ongoing to achieve such a synthetic device.
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Cong, Qiang. "Acylfulvene analogs with spiro-cyclobutane ring and peptide, estrogen prodrugs or illudin /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2004. http://wwwlib.umi.com/cr/ucsd/fullcit?p3123660.

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Tewari, Kunal Mahesh. "Targeted dendrimeric prodrugs for 5-Aminolaevulinic acid photodynamic therapy." Thesis, University of Bath, 2016. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.715275.

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Photodynamic therapy (PDT) is an emerging therapy for the treatment of cancer and various other human disorders. 5-Aminolaevulinic acid (ALA) is a simple natural product that is of great interest for PDT because it can be converted within cells via the haem biosynthetic pathway to the photosensitiser, protoporphyrin IX (PpIX). ALA-PDT has become a first line clinical approach for the treatment of cancerous and precancerous skin lesions (e.g Bowen’s disease, basal skin carcinomas, and actinic keratosis) that would otherwise require significant conventional surgery. However, ALA being a zwitterion suffers from poor lipid solubility and at the same time has stability issues at physiological or alkaline pH. The work herein describes some novel strategies to enhance the delivery of ALA to specific cell types using targeted ALA dendrimeric prodrugs. Specifically, it describes the synthesis of molecules consisting of branched units with 3 or more copies of ALA attached to a central core structure (e.g. gallic acid) using copper-catalysed azide-alkyne click chemistry (CuAAC). Selective delivery of the dendrimeric ALA cargo was achieved by attachment of a homing peptide to an independently addressable functional group on the prodrug core. As proof of concept of this approach, systems were prepared containing a peptide that allows selective targeting of the epidermal growth factor receptor (EGFR) which is overexpressed in a variety of tumours. Targeted ALA delivery and PpIX production was studied with these prodrugs in EGFR-expressing breast adenocarcinoma cells (MDA-MB-231 cells) and a peptide-targeted derivative with 9 ALA units was found to have enhanced PDT efficacy compared to an equimolar dose of ALA. Other targeting units that have been attached to these dendrimeric ALA prodrugs include biomolecules such as vitamin E, thymidine (a nucleoside) and a glucose derivative. Additionally, strain-promoted azide-alkyne cycloadditions (SPAAC) of the same EGFR-targeting peptide with some classical photosensitisers were also investigated and biological studies in EGFR-overexpressing cell lines were carried out. Lastly, a group of cell penetrating peptide-ALA conjugates have been synthesised via CuAAC as a novel approach for targeted ALA delivery.
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Kotamraj, Phanidhara R. "Binding induced enzyme activated methotrexate-α-peptide prodrugs for integrin targeted drug delivery." Scholarly Commons, 2009. https://scholarlycommons.pacific.edu/uop_etds/2619.

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Improving the therapeutic efficacy and quality of life of patients by reducing the side effects caused by non-specificity of cytotoxic drugs has been a challenge in cancer treatment. A hypothesis was developed where integrin binding induced conformational change in a drug conjugated to hairpin peptide with an integrin binding ligand can lead to preferential accumulation of drug and reduced collateral damage by decreased premature prodrug activation. A model drug, MTX and a tripeptide ligand, RGD, known to specifically bind tumor overexpressing α v β 3 integrin receptors, were selected to test the hypothesis. A twelve amino acid sequence that has been previously shown to preferentially adopt an anti-parallel beta hairpin conformation in aqueous environment was flanked with MTX and RGD on N and C termini respectively by solid phase peptide synthesis to form a labile link between Arg-Glu specifically cleaved by SGPE, a Streptomyces griseus derived endopeptidase. Adenoviral vector was developed using AdEasy system for β 3 cDNA transfection to overexpress integrin α v β 3 receptor. MTX-α-RGD and MTX-β-hairpin-RGD were characterized using MALDI-TOF (MTX-α-RGD, 782.6(M+H + ); MTX-β-hairpin-RGD, 2272.1(M+H + )). Cell adhesion assay using HUVEC and A549 cells that overexpress α v β 3 showed that RGD conjugated prodrugs recognize and preferentially bind to integrin α v β 3 in RGD dependent manner. In rabbit plasma, MTX-β-hairpin-RGD was found to be 3 times more stable than MTX-α-RGD. In the absence of α v β 3 binding, SGPE mediated hydrolysis rate of MTX-β-hairpin-RGD was 0.7±0.1 ng/hr, that was significantly (P<0.025) lower than that of MTX-α-RGD (1.0±0.1ng/hr), a prodrug without hairpin structure. In presence of α v β 3 over-expressing cells, significant increase (P<0.025) in hydrolysis rate of MTX-β-hairpin-RGD to 1.0±0.1 ng/hr was observed, not significantly (P=0.6) different from that of MTX-α-RGD (1.1±0.1ng/hr). In addition, there was 400% increase in the fluorescence when FRET based quenching was abolished by the binding induced unfolding. These experiments along with docking studies using molecular modeling support the binding induced unfolding. Results from this investigation suggest that drugs conjugated to peptide ligands such as RGD may reduce the dose needed to achieve therapeutic concentrations by preferential recognition and binding to overexpressed integrin markers. Secondly, reduction of premature activation of prodrugs and thus reduced collateral damage may be achieved by making the the drug release to occurs preferentially upon binding to cells expressing specific integrin markers.
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Elbakay, Jamal A. M. "Synthesis and pharmacological evaluation of novel anti-tumour prodrugs. Synthesis and pharmacological investigations into novel MMP-activated peptide-based prodrugs of methotrexate as potential cancer therapeutics." Thesis, University of Bradford, 2017. http://hdl.handle.net/10454/15102.

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Elbakay, Jamal Ali Mohamed. "Synthesis and pharmacological evaluation of novel anti-tumour prodrugs : synthesis and pharmacological investigations into novel MMP-activated peptide-based prodrugs of methotrexate as potential cancer therapeutics." Thesis, University of Bradford, 2017. http://hdl.handle.net/10454/15102.

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Methotrexate (MTX) is an antimetabolite anticancer agent that is used in treatment of multiple cancers, such as acute lymphoblastic leukaemia and osteosarcoma. A lack of selective tumour toxicity is one of the major problems associated with MTX chemotherapy, especially when given at high doses, as in high dose MTX (HDMTX) therapy. MTX causes various toxicity problems including life-threatening nephrotoxicity, haematological toxicity and neurotoxicity. Overcoming this toxicity is of great importance and has been attempted in various ways, not least via the design of prodrugs. The concept of tumour protease, and specifically matrix metalloproteinase (MMP), activated prodrugs was the focus of the work described in this thesis. This concept relies upon attachment of an MMP-sensitive peptide sequence to a specific site in a drug structure, so as to inactive it. The activity of the parent drug is restored once it is activated by the MMPs in the tumour microenvironment. In this work, different MMP-sensitive peptide sequences linked to MTX were synthesised, resulting in 63 MTX prodrugs. The MMP-mediated activation of these conjugates in tumour tissues (specifically HT1080 homogenates) ex vivo was assessed and the results were compared to the activation of these conjugates in various normal tissues specifically liver, kidney and lung. Specific criteria were established for the selection of promising conjugates for more detailed study. From 7 promising compounds, compound 75 was identified as the lead prodrug, demonstrating selective MMP activation, as indicated by inhibition of its activation by broad spectrum MMP inhibitor ilomastat. The pharmacokinetics of compound 75 was studied in tumour (HT1080) xenograft-bearing mice and the results were compared to those obtained from administration of equimolar doses of conventional MTX. Compound 75 led to enhanced tumour concentrations of MTX, with reduced exposure to normal tissues in vivo compared to conventional MTX therapy. Furthermore, the efficacy of equimolar doses of compound 75 and directly dosed MTX in reduction of HT1080 volume were compared. Superior antitumour activity was observed with compound 75 compared to MTX treatment. Compound 75 is the first example of an MMP-activated prodrug to be reported with enhanced therapeutic index, as evidenced by a full in vivo pharmacokinetic analysis and normal tissue metabolism data. The data presented in thesis support the concept of MMP-activated prodrug development, and form a strong foundation upon which to develop a clinicallyuseful MTX prodrug, with the potential to enhance efficacy and reduce toxicity to the patient.
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Kansara, Viral Mitra Ashim K. "Ocular delivery of peptide ganciclovir prodrugs following subconjunctival injection evaluation of episcleral drug delivery approach /." Diss., UMK access, 2007.

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Thesis (Ph. D.)--School of Pharmacy. University of Missouri--Kansas City, 2007.
"A dissertation in pharmaceutical sciences and pharmacology." Advisor: Ashim K. Mitra. Typescript. Vita. Title from "catalog record" of the print edition Description based on contents viewed May 23, 2008. Includes bibliographical references (leaves 210-225). Online version of the print edition.
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Twum, Elvis Asare. "Development of prodrugs to deliver super-potent drugs to prostate tumours." Thesis, University of Bath, 2013. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.608329.

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Conventional treatments for prostate cancer have significant limitations making it difficult to control the disease. Cyclopropabenzindoles (CBI) are more biologically potent, stable and synthetically accessible analogues of cyclopropapyrroloindole (CPI) anti-tumour antibiotics, such as duocarmycin-SA and CC1065. A polymeric prodrug carrying a CBI drug attached to the polymeric backbone through a PSA cleavable linker peptide has two modes of selectivity: activation by PSA and the EPR effect. To synthesise a 5-amino-seco-CBI analogue, 2,4-dinitronaphthalen- 1-ol gave di-Boc-1-iodonaphthalene-2,4-diamine in five steps (triflation, SNAr displacement with iodide, reduction (loss of iodine), protection and restoration of the iodine. For the amino-seco-CBI, it was important to discriminate between N2 and N4. Acidic removal of the Boc-group(s) resulted in deiodination. NMR investigations showed an unexpected Wheland-like cationic intermediate. N3 of naphthalene-1,3-diamine was selectively trifluoroacetylated and N1 was masked with Boc. Electrophilic iodination gave an orthogonally protected 1-iodonaphthalene-2,4-diamine. Allylation at the trifluoroacetamide was followed by free radical cyclisation with TEMPO trap. Removal of the trifluoroacetyl group allowed coupling to 5-(2-(dimethylamino)ethoxy)-1H-indole-2-carboxylic acid. Reductive removal of 2,2,6,6-tetramethylpiperidine, substitution of the exposed hydroxy group with chloride and removal of the Boc-group gave the amino-seco-CBI drug, 5-amino-1-chloromethyl-3-(5-(2-dimethylaminoethoxy)indole-2-carbonyl)-2,3-dihydro-1H-benz[e]indole. A DNA-melting assay confirmed that it binds very strongly to dsDNA causing a 13 deg. C increase in melting temperature. The drug was a highly potent cytotoxin in vitro, with IC50 = 18 nM against LNCaP prostate cancer cells. The polymeric prodrug system involved the synthesis of the pentapeptide SSKLQ. The amide side chain of glutamine can be masked as the nitrile and this can be quantitatively hydrated to the γ-carboxamide of L-Gln with hydroperoxide. The pentapeptide was coupled to 4-methoxynaphthalen-1-amine and to poly(ethylene glycol) as a model polymeric prodrug system. Efficient release of the model drug from the polymeric prodrug by PSA will allow this polymeric prodrug system to be adopted for the synthesised amino-seco-CBI drug.
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Youssef, Ahmed M. M. "Pharmacological investigations into matrix metalloproteinase-activated anti-tumour prodrugs. In vitro metabolic and pharmacological investigations into a series of colchicine-based peptide prodrugs activated by tumour-expressed matrix metalloproteinases." Thesis, University of Bradford, 2014. http://hdl.handle.net/10454/13982.

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Books on the topic "Peptide Prodrugs"

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De, Arnab. Application of Peptide-Based Prodrug Chemistry in Drug Development. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-4875-4.

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Symposium Pharmaco-Clinique Roussel Uclaf (19 1995 Paris, France). Peptidomimetics: Structural, biological and pharmacological results : Paris, 30 November and 1st December 1995. Romainville: Institut scientifique Roussel, 1995.

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Application of PeptideBased Prodrug Chemistry in Drug Development Springerbriefs in Pharmaceutical Science Drug Development. Springer, 2012.

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M, Kazmierski Wieslaw, ed. Peptidomimetics protocols. Totowa, NJ: Humana Press, 1999.

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Kazmierski, Wieslaw M. Peptidomimetics Protocols. Humana Press, 2010.

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De, Arnab. Application of Peptide-Based Prodrug Chemistry in Drug Development. Springer London, Limited, 2012.

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Book chapters on the topic "Peptide Prodrugs"

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De, Arnab. "Characterization of Prodrugs." In Application of Peptide-Based Prodrug Chemistry in Drug Development, 31–51. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-4875-4_4.

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Bai, J. P. F., B. H. Stewart, and G. L. Amidon. "Gastrointestinal Transport of Peptide and Protein Drugs and Prodrugs." In Pharmacokinetics of Drugs, 189–206. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78680-8_6.

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Forde, Éanna B., Graeme Kelly, Hisham Makki, Zahraa Al-Sharshahi, Deirdre Fitzgerald-Hughes, and Marc Devocelle. "Using Disease-Associated Enzymes to Activate Antimicrobial Peptide Prodrugs." In Methods in Molecular Biology, 359–68. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6737-7_26.

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Basava, C., L. M. Selk, R. Basava, M. Gardner, S. Parker, D. D. Richman, and K. Y. Hostetler. "Novel peptide prodrugs: Lipid derivatization of protease inhibitor enhances in vivo plasma half life." In Peptides, 837–39. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2_280.

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Borchardt, Ronald T., and Binghe Wang. "Prodrug Strategies to Improve the Oral Absorption of Peptides and Peptide Mimetics." In ACS Symposium Series, 36–45. Washington, DC: American Chemical Society, 2000. http://dx.doi.org/10.1021/bk-2000-0752.ch004.

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Kurtzhals, P., U. Ribel, L. Schäffer, and N. C. Kaarsholm. "Co3+-insulin hexamer is a prodrug of human insulin." In Peptides 1994, 879–80. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_405.

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De, Arnab. "Application of Prodrug Chemistry to GLP-1." In Application of Peptide-Based Prodrug Chemistry in Drug Development, 15–21. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-4875-4_2.

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De, Arnab. "Introduction." In Application of Peptide-Based Prodrug Chemistry in Drug Development, 1–13. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-4875-4_1.

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De, Arnab. "Experimental Procedures." In Application of Peptide-Based Prodrug Chemistry in Drug Development, 23–29. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-4875-4_3.

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De, Arnab. "Conclusion." In Application of Peptide-Based Prodrug Chemistry in Drug Development, 53–60. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-4875-4_5.

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Conference papers on the topic "Peptide Prodrugs"

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Devocelle, Marc, Éanna Forde, André Schütte, Andrea Molero-Bondia, Emer Reeves, Catherine Greene, Hilary Humphreys, Marcus Mall, and Deirdre Fitzgerald-Hughes. "Antimicrobial Peptide Prodrugs and Mimetics." In 2nd International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2016. http://dx.doi.org/10.3390/ecmc-2-a011.

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Mandal, Pijus K., Yanhua Yao, Anne R. Bresnick, Jonathan M. Backer, and John S. McMurray. "Abstract 4838: Peptide prodrugs targeting the SH2 domains of p85 block PI3K signaling." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4838.

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Forde, Eanna, Hilary Humphreys, Catherine Greene, Deirdre Fitzgerald-Hughes, Louise Sweeney, Ronan MacLoughlin, and Marc Devocelle. "LATE-BREAKING ABSTRACT: Host defence peptide prodrugs are respirable when delivered by vibrating mesh nebuliser." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa3888.

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Huang, Mofei, Jing Pan, Qi Zhang, Shizuko Sei, Robert Shoemaker, Ronald Lubet, Yian Wang, Barbara Slusher, and Ming You. "Abstract 440: Potentiation of EGFR peptide cancer vaccine by an orally bioavailable glutamine antagonist prodrug JHU-083." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-440.

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Casazza, Andrea, Massimiliano Mazzone, and Peter Pokreisz. "Abstract 180: PhAc-ALGP-Dox is a new tumor selective peptide prodrug of doxorubicin that shows improved efficacy and systemic tolerance in triple negative breast cancer models." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-180.

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Reports on the topic "Peptide Prodrugs"

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Denmeade, Samuel R. Enzymatic Activation of Peptide Prodrugs by Prostate-Specific Membrane Antigen (PSMA) as Targeted Therapy for Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, January 2003. http://dx.doi.org/10.21236/ada414810.

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Denmeade, Samuel R. Enzymatic Activation of Peptide Prodrugs by Prostate-Specific Membrane Antigen (PSMA) as Targeted Therapy for Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, January 2005. http://dx.doi.org/10.21236/ada460938.

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You might also be interested in the extended bibliographies on the topic 'Peptide Prodrugs' for particular source types:
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