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  • Title: Copper(II) complexes of Neobelliera Bullata Trypsin Modulating Oostatic Factor and its analogues.
    Author: Kowalik-Jankowska T, Biega L, Kuczer M, Konopińska D.
    Journal: J Inorg Biochem; 2008 Aug; 102(8):1615-22. PubMed ID: 18397813.
    Abstract:
    The stoichiometry, stability constants and solution structure of the complexes formed in the reaction of copper(II) with hexapeptide NPTNLH, i.e. the Neobelliera Bullata Trypsin Modulating Oostatic Factor (Neb-TMOF), and its analogues DPTNLH, Ac-NPTNLH and Ac-DPTNLH have been determined by potentiometric, UV-visible, CD and EPR spectroscopic methods. Upon raising pH for Ac-NPTNLH and Ac-DPTNLH peptides, copper(II) coordination starts from the imidazole nitrogen of the His(6); afterwards three deprotonated amide nitrogens are progressively involved in metal ions coordination. In a wide pH range of 4.5-8.5 for the NPTNLH and DPTNLH ligands the CuL complex dominates with the imidazole nitrogen of His(6) coordinated to form a macrochelate. The N-terminal amino group of the NPTNLH and DPTNLH peptides takes part in the coordination of the metal ion in the CuL, CuH(-1)L and CuH(-2)L complexes. However, at pH above 9 the CuH(-3)L complex with the {N(Im),3N(-)} coordination mode is formed. For the CuH(-2)L complex the spectroscopic data clearly indicate the 4N {NH(2), CO or COO(-), 2N(-), N(Im)} bonding mode with the axial coordination of the N-terminal amine group to the metal ion.
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