Apinya BuranaprapukParin ChaivisuthangkuraJisnuson SvastiChalla V. KumarSrinakharinwirot UniversityMahidol UniversityUniversity of Connecticut2018-06-212018-06-212005-09-01Letters in Organic Chemistry. Vol.2, No.6 (2005), 554-558157017862-s2.0-46149087568https://repository.li.mahidol.ac.th/handle/20.500.14594/16298Photocleavage of -lysozyme and bovine serum albumin (BSA) by L-phenylalanine-1(1-pyrene) methylamide (PMA-L-Phe) is reported here. The chiral probe, PMA-L-Phe, has a positively charged side chain, while the previous probes carried a free carboxyl group. The yield of lysozyme cleavage by PMA-L-Phe is increased to 57% when compared to the previous probes, while the yield of BSA cleavage is reduced to <5%. Sequencing studies indicated that PMA-L-Phe cleaves lysozyme at a single site, between residues Trp108-Va1109. Absorption and fluorescence spectral data indicate that PMA-L-Phe binds to lysozyme and BSA with affinity constants (Kb) of 3.3×105 M-1 and 3.8×105 M-1, respectively. © 2005 Bentham Science Publishers Ltd.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyChemistryReviewSCOPUS10.2174/1570178054640868