1,444
Views
14
CrossRef citations to date
0
Altmetric
Research Article

Synthesis and structural analysis of halogen substituted fibril formation inhibitors of Human Transthyretin (TTR)

, , , &
Pages 40-51 | Received 15 Jan 2016, Accepted 14 Mar 2016, Published online: 11 Apr 2016

References

  • Blake CC, Geisow MJ, Oatley SJ, et al. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J Mol Biol 1978;121:339–56.
  • Wojtczak A, Cody V, Luft JR, Pangborn W. Structures of human transthyretin complexed with thyroxine at 2.0 A resolution and 3′,5′-dinitro-N-acetyl-l-thyronine at 2.2 A resolution. Acta Crystallogr D Biol Crystallogr 1996;52:758–65.
  • Kanai M, Raz A, Goodman DS. Retinol-binding protein: the transport protein for vitamin A in human plasma. J Clin Invest 1968;47:2025–44.
  • Soprano DR, Herbert J, Soprano KJ, et al. Demonstration of transthyretin mRNA in the brain and other extrahepatic tissues in the rat. J Biol Chem 1985;260:11793–8.
  • Landers KA, Mortimer RH, Richard K. Transthyretin and the human placenta. Placenta 2013;34:513–17.
  • Purdy RH, Woeber KH, Holloway MT, Ingbar SH. Preparation of crystalline thyroxine-binding prealbumin from human plasma. Biochemistry 1965;4:1888–95.
  • Buxbaum JN, Tagoe CE. The genetics of the amyloidoses. Annu Rev Med 2000;51:543–69.
  • Westermark P, Sletten K, Johansson B, Cornwell GG. Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci USA 1990;87:2843–5.
  • Pilato E, Dell’Amore A, Botta L, Arpesella G. Combined heart and liver transplantation for familial amyloidotic neuropathy. Eur J Cardiothorac Surg 2007;32:180–2.
  • Ohya Y, Okamoto S, Tasaki M, et al. Manifestations of transthyretin-related familial amyloidotic polyneuropathy: long-term follow-up of Japanese patients after liver transplantation. Surg Today 2011;41:1211–18.
  • Almeida MR, Cardoso I, Saraiva MJ. In vitro and in vivo effects of genistein on TTR stabilization and aggregation. In: Skinner M, Berk JL, Connors LH, Seldin DC, eds. XIth International symposium on amyloidosis. Boca Raton (FL): CRC Press; 2007:113.
  • Connelly S, Choi S, Johnson SM, et al. Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses. Curr Opin Struct Biol 2010;20:54–62.
  • Ferguson RN, Edelhoch H, Saroff HA, et al. Negative cooperativity in the binding of thyroxine to human serum prealbumin. Preparation of tritium-labeled 8-anilino-1-naphthalenesulfonic acid. Biochemistry 1975;14:282–9.
  • Neumann P, Cody V, Wojtczak A. Structural basis of negative cooperativity in transthyretin. Acta Biochim Pol 2001;48:867–75.
  • Herbert J, Wilcox JN, Pham K-TC, et al. Transthyretin: a choroid plexus-specific transport protein in human brain. The 1986 S. Weir Mitchell award. Neurology 1986;36:90011.
  • Klabunde T, Petrassi HM, Oza VB, et al. Rational design of potent human transthyretin amyloid disease inhibitors. Nat Struct Biol 2000;7:312–21.
  • Ong DST, Kelly JW. Chemical and/or biological therapeutic strategies to ameliorate protein misfolding diseases. Curr Opin Cell Biol 2011;23:231–8.
  • Nencetti S, Orlandini E. TTR fibril formation inhibitors: is there a SAR? Curr Med Chem 2012;19:2356–79.
  • Coelho T, Maia LF, Da Silva AM, et al. Long-term effects of tafamidis for the treatment of transthyretin familial amyloid polyneuropathy. J Neurol 2013;260:2802–14.
  • Berk JL, Suhr OB, Obici L, et al. Repurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trial. JAMA 2013;310:2658–67.
  • Obici L, Merlini G. An overview of drugs currently under investigation for the treatment of transthyretin-related hereditary amyloidosis. Expert Opin Investig Drugs 2014;23:1239–51.
  • Palaninathan SK, Mohamedmohaideen NN, Orlandini E, et al. Novel transthyretin amyloid fibril formation inhibitors: synthesis, biological evaluation, and X-ray structural analysis. PLoS One 2009;4:e6290.
  • Ciccone L, Nencetti S, Rossello A, et al. X-ray crystal structure and activity of fluorenyl-based compounds as transthyretin fibrillogenesis inhibitors. J Enzyme Inhib Med Chem 2015. [Epub ahead of print]. DOI: 10.3109/14756366.2015.1070265.
  • Dolado I, Nieto J, Saraiva MJM, et al. Kinetic assay for high-throughput screening of in vitro transthyretin amyloid fibrillogenesis inhibitors. J Comb Chem 2005;7:246–52.
  • Oza VB, Smith C, Raman P, et al. Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors. J Med Chem 2002;45:321–32.
  • Stura EA, Nemerow GR, Wilson IA. Strategies in the crystallization of glycoproteins and protein complexes. J Cryst Growth 1992;122:273–85.
  • Ciccone L, Tepshi L, Nencetti S, Stura EA. Transthyretin complexes with curcumin and bromo-estradiol: evaluation of solubilizing multicomponent mixtures. N Biotechnol 2015;32:54–64.
  • Stura EA, Wilson IA. Applications of the streak seeding technique in protein crystallization. J Cryst Growth 1991;110:270–82.
  • Ciccone L, Vera L, Tepshi L, et al. Multicomponent mixtures for cryoprotection and ligand solubilization. Biotechnol Reports 2015;7:120–7.
  • Vera L, Stura EA. Strategies for protein cryocrystallography. Cryst Growth Des 2014;14:427–35.
  • Newman J. Novel buffer systems for macromolecular crystallization. Acta Crystallogr D Biol Crystallogr 2004;60:610–12.
  • Diederichs K, Karplus PA. Better models by discarding data? Acta Crystallogr D Biol Crystallogr 2013;69:1215–22.
  • Adams PD, Afonine PV, Bunkóczi G, et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 2010;66:213–21.
  • Stura EA, Satterthwait AC, Calvo JC, et al. Reverse screening. Acta Crystallogr D Biol Crystallogr 1994;50:448–55.
  • Duran D, Couster SL, Desjardins K, et al. PROXIMA 2A – a new fully tunable micro-focus beamline for macromolecular crystallography. J Phys Conf Ser 2013;425:012005. doi: http://dx.doi.org/10.1088/17426596/425/1/012005.
  • Murshudov GN, Skubák P, Lebedev AA, et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 2011;67:355–67.
  • Emsley P, Lohkamp B, Scott WG, Cowtan K. Features and development of Coot. Acta Crystallogr D Biol Crystallogr 2010;66:486–501.
  • Winn MD, Ballard CC, Cowtan KD, et al. Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 2011;67:235–42.
  • Holbro T, Tagmann E. Bromofluoranthenes II. Synthesis of 4,11-dibromofluoranthene. Helv Chim Acta 1950;33:2178–85.
  • Pan H-L, Fletcher TL. Derivatives of fluorene. XXX. Rearrangement and antitumor activities of some 9-oxofluorene oximes. 6(5H)-Phenanthridinones. J Med Chem 1969;12:822–5.
  • Moore FJ, Huntress EH. Unsymmetrical phenanthridones. 11. A new preparative method: 7-nitrophenanthridone by Beckmann rearrangement of 2-nitrofluorenone oxime. J Am Chem Soc 1927;49:2618–24.
  • Lachman A. Benzophenone oxime. Org Synth 1930;10:10–11.
  • Ulbrich HK, Luxenburger A, Prech P, et al. A novel class of potent nonglycosidic and nonpeptidic pan-selectin inhibitors. J Med Chem 2006;49:5988–99.
  • Dunlop RD, Gardner JH. The preparation of 4-fluoro- and 4,4′-difluorobenzophenone. J Am Chem Soc 1933;55:1665–6.
  • Novak L, Protiva M. Antihistaminic substances L. Derivatives of N-(1-indanyl)ethylenediamine Coll. Czech Chem Commun 1962;27:2413–18.
  • Cianci M, Folli C, Zonta F, et al. Structural evidence for asymmetric ligand binding to transthyretin. Acta Crystallogr D Biol Crystallogr 2015;71:1582–92.
  • Polsinelli I, Nencetti S, Shepard W, et al. A new crystal form of human transthyretin obtained with a curcumin derived ligand. J Struct Biol 2016;194:8–17.
  • Trivella DBB, Bleicher L, Palmieri LDC, et al. Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding. J Struct Biol 2010;170:522–31.
  • Lima LMTR, Silva VDA, Palmieri LDC, et al. Identification of a novel ligand binding motif in the transthyretin channel. Bioorg Med Chem 2010;18:100–10.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.