Tetracycline inhibits W7FW14F apomyoglobin fibril extension and keeps the amyloid protein in a pre-fibrillar, highly cytotoxic state Clorinda Malmo * , Silvia Vilasi † , Clara Iannuzzi * , Silvia Tacchi † , Cesare Cametti ‡ , Gaetano Irace * and Ivana Sirangelo * ,1 * Dipartimento di Biochimica e Biofisica, Seconda Università di Napoli, Naples, Italy; † Dipartimento di Fisica, Università di Perugia, Perugia, Italy; and ‡ Dipartimento di Fisica, Università di Roma "La Sapienza, Rome, Italy 1 Corresponding author: Dipartimento di Biochimica e Biofisica, Seconda Università di Napoli, Via L. De Crecchio 7, Napoli 80138, Italy. E-mail: ivana.sirangelo@unina2.it <h3>SPECIFIC AIMS</h3> Our aim was to test the general potentiality of tetracycline as antiamyloidogenic agent probing its effect on the amyloid forming apomyoglobin mutant W7FW14F. <h3>PRINCIPAL FINDINGS</h3> <h3>1. Tetracycline inhibits W7FW14F apomyoglobin fibrillogenesis</h3> We monitored the effect of tetracycline on fibril formation by using thioflavin T (ThT) fluorescence assay, atomic force microscopy (AFM), and light-scattering. Early apomyoglobin aggregates were incubated with tetracycline at a protein/drug molar ratio of 1:5 and aliquots of sample were tested for ThT fluorescence assay at different times. Tetracycline inhibited the ThT fluorescence increase normally observed on time. The morphological features induced by incubation
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