Conformation-dependent affinity of Cu(II) ions peptide complexes derived from the human Pin1 protein : ITC and DSC study

Dorota Uber , Dariusz Wyrzykowski , Caterina Tiberi , Giuseppina Sabatino , Wioletta Żmudzińska , Lech Chmurzyński , Anna Maria Papini , Joanna Makowska

Abstract

The human Pin1 WW domain catalyzes the cis – trans isomerization of the proline peptide bond. In this study, the conformation and binding of Cu(II) ions by Pin1 were investigated. It has been found that the affinity of peptide fragments of the human Pin1 WW domain for Cu(II) ions depends on its conformation. In particular, we analyzed three peptides derived from human Pin1: the nonapeptide hPin1(14–22) (with sequence Arg-Met-Ser- Arg-Ser-Ser-Gly-Arg-Val-NH 2 , peptide 1) the undecapep- tide hPin1(13–23) (with sequence Lys-Arg-Met-Ser-Arg- Ser-Ser-Gly-Arg-Val-Tyr-NH 2 , peptide 2) and its deriva- tive Ala13Ala23hPin1(13–23) (with sequence Ala-Arg- Met-Ser-Arg-Ser-Ser-Gly-Arg-Val-Ala-NH 2 , peptide 3) to study the role of presence in the sequence of the flanked residues at the N- and C-terminus, i.e., Lys13 and Tyr23. The presence of heat-capacity peaks found by DSC mea- surements for the systems studied strongly suggests that the conformational equilibria of the peptides studied strongly depend on the temperature. NMR spectroscopy and molecular dynamics simulations were instrumental to ver- ify the conformational preferences of three peptides. The absence of likely or oppositely charged groups at the ends of a short chain fragment destroys chain reversal because the charged groups probably screen the nonpolar core from the solvent. ITC experiment was used to study the inter- actions with Cu(II) ions. It was found that the most stable complexes with Cu 2 ? ions are formed with peptide 2, which has the most bent conformation.
Author Dorota Uber PFZK
Dorota Uber ,,
- Laboratory of Physicochemistry of Coordination Complexes
, Dariusz Wyrzykowski PFZK
Dariusz Wyrzykowski,,
- Laboratory of Physicochemistry of Coordination Complexes
, Caterina Tiberi
Caterina Tiberi,,
-
, Giuseppina Sabatino
Giuseppina Sabatino,,
-
, Wioletta Żmudzińska PSB
Wioletta Żmudzińska,,
- Laboratory of Biopolymers Structure
, Lech Chmurzyński PFZK
Lech Chmurzyński,,
- Laboratory of Physicochemistry of Coordination Complexes
, Anna Maria Papini
Anna Maria Papini,,
-
, Joanna Makowska PFZK
Joanna Makowska,,
- Laboratory of Physicochemistry of Coordination Complexes
Journal seriesJournal of Thermal Analysis and Calorimetry, ISSN 1388-6150
Issue year2017
Vol127
No2
Pages1431-1443
Publication size in sheets0.6
Keywords in Englishpeptide conformation, β-hairpin, hPin1 peptides, NMR
DOIDOI:10.1007/s10973-016-5387-9
URL http://link.springer.com/content/pdf/10.1007%2Fs10973-016-5387-9.pdf
Languageen angielski
Score (nominal)25
ScoreMinisterial score = 20.0, 20-12-2017, ArticleFromJournal
Ministerial score (2013-2016) = 25.0, 20-12-2017, ArticleFromJournal
Publication indicators WoS Impact Factor: 2016 = 1.953 (2) - 2016=1.69 (5)
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