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• W2022743059 abstract "Among our studies concerning the coordination chemistry of naturally occurring peptides we have been studying recently metal ion interaction with two hypothalamic hormones: thyroliberin (TRF) and melanostatin (MIF). These two hormones are the only tripeptides among all the pituitary hormones described until now [1–4]. TRF (PyrHisProNH2) and MIF (ProLeuGlyNH2) have been extensively studied in various biological aspects [5], among others their possible use in the clinical treatment of metal diseases [6]. Many hormone analogues have been synthesized in order to solve the problem of the relation between biological activity and chemical structure [7]. In most papers the critical role of the histidine residue in TRF biological activity is suggested. Our main interest concerns the coordination abilities of both hormones and some of their analogues and the relation between the binding modes and the ligand conformation (structure). Spectroscopic (NMR, EPR, absorption and CD spectra) and potentiometric techniques were used to solve these problems. Though the MIF binding mode to Cu(II) and Ni(II) ions looks classical, the strongly basic Pro nitrogen donor on the N-terminal leads to the formation of very low concentration of 110 (1N) complex species [8]. The histidine residue of TRF ligand is a major binding site of metal ions. The other two residues however, have a critical importance for the complex equilibria and the structure of the formed species [9, 10]. The replacement of pyroglutamic acid with picolinic acid in the TRF molecule causes a major change in the structure of its Cu(II) and Ni(II) complexes. E.g., in the Cu(II)PicHis system a very specific equilibrium between dimeric and monomeric species was observed [11]. The introduction of tyrosine residue in the TRF sequence in place of histidine also changes the peptide coordination ability. In the Ni(II)PyrTyrProNH2 system a direct involvement of ProNH2 residue in the metal binding was proposed [11]. TRF analogue with nicotinic acid in place of pyroglutamic acid forms very unstable Cu(II) complexes due to the unfavourable meta-position of the nitrogen donor with respect to carbonyl in the pyridine ring. Also the TRF analogue with ProNHNH2 residue in the C-terminal position forms much weaker Cu(II) and Ni(II) complexes than the TRF peptide. The studies which were done for both hormones show that naturally occurring peptides may form relatively strong complexes with some metal ions and their chemical and physical properties may be very specific for each ligand. The latter conclusion becomes evident when the coordination abilities of the different chemical analogues (e.g. of TRF) are compared." @default.
• W2022743059 created "2016-06-24" @default.
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• W2022743059 date "1983-01-01" @default.
• W2022743059 modified "2023-09-25" @default.
• W2022743059 title "Interaction of metal ions with peptide hormones" @default.
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• W2022743059 doi "https://doi.org/10.1016/s0020-1693(00)95318-0" @default.
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