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

Content Provider	Springer Nature Link
Author	Uber, Dorota Wyrzykowski, Dariusz Tiberi, Caterina Sabati, Giuseppina Żmudzińska, Wioletta Chmurzyński, Lech Papini, Anna Maria Makowska, Joanna
Copyright Year	2016
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 undecapeptide hPin1(13–23) (with sequence Lys-Arg-Met-Ser-Arg-Ser-Ser-Gly-Arg-Val-Tyr-NH$_{2}$, peptide 2) and its derivative 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 measurements 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 verify 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 interactions 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.
Starting Page	1431
Ending Page	1443
Page Count	13
File Format	PDF
ISSN	13886150
Journal	Journal of thermal analysis
Volume Number	127
Issue Number	2
e-ISSN	15882926
Language	English
Publisher	Springer Netherlands
Publisher Date	2016-04-04
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Peptide conformation β-Hairpin hPin1 peptides NMR Physical Chemistry Analytical Chemistry Polymer Sciences Inorganic Chemistry Measurement Science and Instrumentation
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry Condensed Matter Physics

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