Protein Information

ID 1428
Name transthyretin
Synonyms ATTR; HsT2651; PALB; Prealbumin; TBPA; TTR; Transthyretin; Transthyretin precursor…

Compound Information

ID 1403
Name naphthalene
CAS naphthalene

Reference

PubMed Abstract RScore(About this table)
17630783 Wilkinson-White LE, Easterbrook-Smith SB: Characterization of the binding of Cu (II) and Zn (II) to transthyretin: effects on amyloid formation. Biochemistry. 2007 Aug 7;46(31):9123-32. Epub 2007 Jul 14.
Although metal ions can promote amyloid formation from many proteins, their effects on the formation of amyloid from transthyretin have not been previously studied. We therefore screened the effects of Cu (II), Zn (II), Al (III), and Fe (III) on amyloid formation from wild-type (WT) transthyretin as well as its V30M, L55P, and T119M mutants. Cu (II) and Zn (II) promoted amyloid formation from the L55P mutant of transthyretin at pH 6.5 but had little effect on amyloid formation from the other forms of the protein. Zn (II) promoted L55P amyloid formation at pH 7.4 but Cu (II) inhibited it. Cu (II) gave dose-dependent quenching of the tryptophan fluorescence of transthyretin and the fluorescence of 1-anilino-8-naphthalene sulfonate bound to it. Zn (II) gave dose-dependent quenching of the tryptophan but not the 1-anilino-8-naphthalene sulfonate fluorescence. Apparent dissociation constants for Cu (II) and Zn (II) binding at pH 7.4 of approximately 10 nM and approximately 1 microM (approximately 0.4 microM and approximately 5 microM at pH 6.5), respectively, were obtained from the quenching data. Zn (II) enhanced urea-mediated the dissociation of the L55P but not the WT transthyretin tetramer. Cu (II), depending on its concentration, either had no effect or stabilized the WT tetramer but could enhance urea-mediated dissociation of L55P.
34(0,1,1,4)