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Title:          PITB: A high affinity transthyretin aggregation inhibitor with optimal pharmacokinetic properties
Subject:        European Journal of Medicinal Chemistry, 261 (2023) 115837. doi:10.1016/j.ejmech.2023.115837
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      Title: PITB: A high affinity transthyretin aggregation inhibitor with optimal pharmacokinetic properties
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        Title: 1 Introduction
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          Title: 2.1 Rational design and synthesis of PITB
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          Title: 2.2 PITB kinetically stabilizes TTR in vitro
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          Title: 2.3 PITB protects TTR from aggregation in vitro
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          Title: 2.4 PITB binds with high affinity to TTR
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          Title: 2.5 PITB stabilizes the weaker TTR dimer-dimer interface
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          Title: 2.6 PITB selectively binds and stabilizes WT-TTR and V30M-TTR in human plasma
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          Title: 2.7 PITB displays no toxicity for human cells
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          Title: 2.8 PK studies in mice confirm the bioavailability and stability of PITB
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        Title: 3 Conclusion
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        Title: 4 Experimental section
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          Title: 4.2 Synthesis procedure
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            Title: 4.2.1 (3,4-Dimethoxy-5-nitrophenyl) (3-fluoro-5 methoxyphenyl)methanone (3)
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            Title: 4.2.2 (3-fluoro-5-hydroxyphenyl) (4-hydroxy-3-methoxy-5-nitrophenyl)methanone, PITB
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          Title: 4.3 Recombinant TTR expression and purification
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          Title: 4.4 Urea-induced TTR tetramer dissociation measured by Trp fluorescence
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          Title: 4.5 TTR in vitro aggregation inhibition
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          Title: 4.6 Isothermal titration calorimetry
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          Title: 4.11 In vivo pharmacokinetic studies in mice
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        Title: Declaration of competing interest
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        Title: Data availability
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        Title: Acknowledgements
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        Title: Appendix A Supplementary data
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        Title: References
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  Checksum: 874ae09e
   Type: CRC32
  Checksum: bbc94bab1788cbdb9c441ddf009e21cc
   Type: MD5
  Checksum: 0671cb418a480ea2a6dfbe6a39909a1b126ceb48
   Type: SHA-1