Department of Chemistry, University of Southern California, Los Angeles, California 90089-0744, USA.
Mol Pharm. 2010 Dec 6;7(6):2349-61. doi: 10.1021/mp100186b. Epub 2010 Oct 7.
Cidofovir (HPMPC), a broad spectrum antiviral agent, cannot be administered orally due to ionization of its phosphonic acid group at physiological pH. One prodrug approach involves conversion to the cyclic form (cHPMPC, 1) and esterification by the side chain hydroxyl group of a peptidomimetic serine. Transport studies in a rat model have shown enhanced levels of total cidofovir species in the plasma after oral dosing with L-Val-L-Ser-OMe cHPMPC, 2a. To explore the possibility that 2a and its three L/D stereoisomers 2b-d undergo active transport mediated by the peptide-specific intestinal transporter PEPT1, we performed radiotracer uptake and electrophysiology experiments applying the two-electrode voltage clamp technique in Xenopus laevis oocytes overexpressing human PEPT1 (hPEPT1, SLC15A1). 2a-d did not induce inward currents, indicating that they are not transported, but the stereoisomers with an L-configuration at the N-terminal valine (2a and 2b) potently inhibited transport of the hPEPT1 substrate glycylsarcosine (Gly-Sar). A "reversed" dipeptide conjugate, L-Ser-L-Ala-OiPr cHPMPC (4), also did not exhibit detectable transport, but completely abolished the Gly-Sar signal, suggesting that affinity of the transporter for these prodrugs is not impaired by a proximate linkage to the drug in the N-terminal amino acid of the dipeptide. Single amino acid conjugates of cHPMPC (3a and 3b) or cHPMPA (5, 6a and 6b) were not transported and only weakly inhibited Gly-Sar transport. The known hPEPT1 prodrug substrate valacyclovir (7) and its L-Val-L-Val dipeptide analogue (8) were used to verify coupled transport by the oocyte model. The results indicate that the previously observed enhanced oral bioavailability of 2a relative to the parent drug is unlikely to be due to active transport by hPEPT1. Syntheses of the novel compounds 2b-d and 3-6 are described, including a convenient solid-phase method to prepare 5, 6a and 6b.
西多福韦(HPMPC)是一种广谱抗病毒药物,由于其磷酸基团在生理 pH 下发生离子化,因此不能口服给药。一种前药方法是将其转化为环状形式(cHPMPC,1),并通过肽模拟丝氨酸的侧链羟基酯化。在大鼠模型中的转运研究表明,口服给予 L-Val-L-Ser-OMe cHPMPC(2a)后,血浆中环西多福韦总浓度升高。为了探讨 2a 及其三个 L/D 立体异构体 2b-d 是否通过肠道肽特异性转运体 PEPT1 进行主动转运,我们应用双电极电压钳技术在过表达人 PEPT1(hPEPT1,SLC15A1)的非洲爪蟾卵母细胞中进行放射性示踪摄取和电生理学实验。2a-d 不诱导内向电流,表明它们不能被转运,但 N 末端缬氨酸具有 L-构型的立体异构体(2a 和 2b)强烈抑制 hPEPT1 底物甘氨酰肌氨酸(Gly-Sar)的转运。一种“反向”二肽缀合物,L-Ser-L-Ala-OiPr cHPMPC(4)也没有可检测的转运,但完全阻断了 Gly-Sar 信号,表明这些前药与转运体的亲和力不会因在二肽的 N 末端氨基酸中与药物的邻近连接而受损。cHPMPC 的单氨基酸缀合物(3a 和 3b)或 cHPMPA(5、6a 和 6b)均未被转运,且对 Gly-Sar 转运的抑制作用较弱。已知的 hPEPT1 前药底物伐昔洛韦(7)及其 L-Val-L-Val 二肽类似物(8)用于验证卵母细胞模型的偶联转运。结果表明,与母体药物相比,先前观察到的 2a 口服生物利用度的提高不太可能是由于 hPEPT1 的主动转运。描述了新型化合物 2b-d 和 3-6 的合成,包括一种制备 5、6a 和 6b 的方便固相方法。