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In this study we described the design, rational synthesis and functional characterization of a novel radiolabeled hydrolysis-resistant high-affinity substrate for H + ⁄peptide cotransporters. l-4,4¢-Biphenylalanyl–l-Proline (Bip-Pro) was synthesized according to standard procedures in peptide chemistry. | ỊFEBS Journal Synthesis and characterization of a new and radiolabeled high-affinity substrate for H peptide cotransporters Ilka Knutter1 Bianka Hartrodt2 Geza Toth3 Attila Keresztes3 Gabor Kottra4 Carmen Mrestani-Klaus2 Ilona Born2 Hannelore Daniel4 Klaus Neubert2 and Matthias Brandsch1 1 Biozentrum of the Martin-Luther-University Halle-Wittenberg Halle Germany 2 Institute of Biochemistry Biotechnology Faculty of Sciences I Martin-Luther-University Halle-Wittenberg Halle Germany 3 Institute of Biochemistry BiologicalResearch Center of the Hungarian Academy of Sciences Szeged Hungary 4 Molecular Nutrition Unit TechnicalUniversity of Munich Freising-Weihenstephan Germany Keywords Caco-2 HVpeptide cotransporter 1 HVpeptide cotransporter 2 SKPT Xenopus laevis oocytes Correspondence M. Brandsch Biozentrum of the Martin-Luther-University Halle-Wittenberg Membrane Transport Group Weinbergweg 22 D-06120 Halle Germany Fax 49 345 5527258 Tel 49 345 5521630 E-mail matthias.brandsch@ biozentrum.uni-halle.de Received 15 August 2007 revised 19 September 2007 accepted 20 September 2007 doi 10.1111 j.1742-4658.2007.06113.x In this study we described the design rational synthesis and functional characterization of a novel radiolabeled hydrolysis-resistant high-affinity substrate for H peptide cotransporters. i.-4.4 -Biphenylalanyl L-Proline Bip-Pro was synthesized according to standard procedures in peptide chemistry. The interaction of Bip-Pro with H peptide cotransporters was determined in intestinal Caco-2 cells constitutively expressing human H peptide cotransporter 1 PEPT1 and in renal SKPT cells constitutively expressing rat H peptide cotransporter 2 PEPT2 . Bip-Pro inhibited the 14C Gly-Sar uptake via PEPT1 and PEPT2 with exceptional high affinity Ki 24 IM and 3.4 M respectively in a competitive manner. By employing the two-electrode voltage clamp technique in Xenopus laevis oocytes expressing PEPT1 or PEPT2 it was found that Bip-Pro was transported by both peptide .
