The Experts below are selected from a list of 324 Experts worldwide ranked by ideXlab platform

Ling Song - One of the best experts on this subject based on the ideXlab platform.

Jian Zhou - One of the best experts on this subject based on the ideXlab platform.

Hisashi Yamamoto - One of the best experts on this subject based on the ideXlab platform.

Yongying Jiang - One of the best experts on this subject based on the ideXlab platform.

  • peptide conjugates of 4 aminocyclophosphamide as prodrugs of Phosphoramide mustard for selective activation by prostate specific antigen psa
    Bioorganic & Medicinal Chemistry, 2013
    Co-Authors: Yongying Jiang
    Abstract:

    Abstract In our continued effort to develop prodrugs of Phosphoramide mustard, conjugates of 4-aminocyclophosphamide (4-NH 2 -CPA) with three PSA-specific peptides were synthesized and evaluated as substrates of PSA. These include conjugates of cis -(2 R ,4 R )-4-NH 2 -CPA with a tetrapeptide Succinyl-Ser-Lys-Leu-Gln-OH, a hexapeptide Succinyl-His-Ser-Ser-Lys-Leu-Gln-OH, and a pentapeptide Glutaryl-Hyp-Ala-Ser-Chg-Gln-OH. These conjugates were cleaved by PSA efficiently and exclusively after the expected glutamine residue to release 4-NH 2 -CPA, the activated prodrug form of Phosphoramide mustard. The cleavage was most efficient for the pentapeptide conjugate 3 (Glutaryl-Hyp-Ala-Ser-Chg-Gln-NH-CPA), which showed a half-life of 55 min with PSA, followed by the hexapeptide conjugate 2 (Succinyl-His-Ser-Ser-Lys-Leu-Gln-NH-CPA) and the tertrapeptide conjugate 1 (Succinyl-Ser-Lys-Leu-Gln-NH-CPA) with half-lives of 6.5 and 12 h, respectively. These results indicate a potential of the conjugate 3 as an anticancer prodrug of Phosphoramide mustard for selective PSA activation.

  • synthesis and stereochemical preference of peptide 4 aminocyclophosphamide conjugates as potential prodrugs of Phosphoramide mustard for activation by prostate specific antigen psa
    Bioorganic & Medicinal Chemistry Letters, 2009
    Co-Authors: Yongying Jiang, Robert S Dipaola
    Abstract:

    In an effort to develop proteolytically activated prodrugs of Phosphoramide mustard by prostate-specific antigen (PSA), a series of tetrapeptide (Cbz-Ser-Ser-Phe-Tyr)-conjugated 4-aminocyclophosphamide (4-NH(2)-CPA) isomers were synthesized and evaluated as substrates of PSA. The cleavage of the conjugates by PSA were found to be stereoselective as only the two isomers with 4R-configuration were efficiently cleaved by PSA. The cis-(2R,4R)-isomer was the best substrate of PSA with a half-life of 12min. LC/MS analysis of the incubation solution of this isomer with PSA suggests that 4-NH(2)-CPA is released upon proteolysis and quickly degrades to cytotoxic Phosphoramide mustard. These results clarified the stereochemical requirements of PSA on the peptide conjugates of 4-NH(2)-CPA and demonstrated the potential of these conjugates as potential PSA-activated prodrugs targeting prostate cancer.

  • n 2 2 dimethyl 2 2 nitrophenyl acetyl 4 aminocyclophosphamide as a potential bioreductively activated prodrug of Phosphoramide mustard
    Bioorganic & Medicinal Chemistry Letters, 2008
    Co-Authors: Yongying Jiang
    Abstract:

    N-(2,2-Dimethyl-2-(2-nitrophenyl)acetyl)-4-aminocyclophosphamide isomers (DMNA-NH-CPA, 4) were synthesized stereospecifically from Boc-L-Hse(OBn)-OH and the degradation of the corresponding reduced amine 5a was investigated by UV/vis spectroscopy and LC/MS. The rate of cyclization of 5a was found to increase with decreasing pH, with half-lives ranging from 3.2 to 54 min at pH 4-7.4, suggesting that the cyclization is catalyzed by the hydronium ions. LC/MS analysis of the degradation products of 5a indicates that 4-aminocyclophosphamide is rapidly released from 4 upon reductive activation under acidic conditions and further decomposes into the cytotoxic Phosphoramide mustard. These results validated 4-aminocyclophosphamide as a prodrug form of Phosphoramide mustard and suggest that compound 4 can potentially be used as a prodrug of Phosphoramide mustard for bioreductive activation.

  • Nitroaryl Phosphoramides as novel prodrugs for E. coli nitroreductase activation in enzyme prodrug therapy.
    Journal of Medicinal Chemistry, 2003
    Co-Authors: Yongying Jiang, Jiye Han, Patrick Browne, Peter F. Searle, Paul R. Race, Richard J. Knox, Eva I. Hyde
    Abstract:

    Cyclic and acyclic nitroaryl Phosphoramide mustard analogues were activated by E. coli nitroreductase, an enzyme explored in GDEPT. The more active acyclic 4-nitrobenzyl Phosphoramide mustard (7) showed 167 500x selective cytotoxicity toward nitroreductase-expressing V79 cells with an IC(50) as low as 0.4 nM. This is about 100x more active and 27x more selective than CB1954 (1). The superior activity was attributed to its better substrate activity (k(cat)/K(m) 19x better than 1) and/or excellent cytotoxicity of Phosphoramide mustard released.

Huayin Huang - One of the best experts on this subject based on the ideXlab platform.