High stability and biological activity of the copper(II) complexes of alloferon 1 analogues containing tryptophan.
PBN-AR
Instytucja
Wydział Chemii (Uniwersytet Wrocławski)
Informacje podstawowe
Główny język publikacji
en
Czasopismo
Journal of Inorganic Biochemistry
ISSN
0162-0134
EISSN
0162-0134
Wydawca
Elsevier Science, New York
Rok publikacji
2016
Numer zeszytu
Strony od-do
147-161
Numer tomu
163
Liczba arkuszy
Autorzy
Pozostali autorzy
+ 3
Słowa kluczowe
en
Biological activity
Copper(II) complexes
Stability constants
Tryptophan analogues of alloferon 1
Streszczenia
Język
en
Treść
Copper(II) complex formation processes between the alloferon 1 (Allo1) (HGVSGHGQHGVHG) analogues where the tryptophan residue is introducing in the place His residue H1W, H6W, H9W and H12W have been studied by potentiometric, UV-visible, CD and EPR spectroscopic, and MS methods. For all analogues of alloferon 1 complex speciation have been obtained for a 1:1 metal-to-ligand molar ratio and 2:1 of H1W because of precipitation at higher (2:1, 3:1 and 4:1) ratios. At physiological pH7.4 and a 1:1 metal-to-ligand molar ratio the tryptophan analogues of alloferon 1 form the CuH-1L and/or CuH-2L complexes with the 4N binding mode. The introduction of tryptophan in place of histidine residues changes the distribution diagram of the complexes formed with the change of pH and their stability constants compared to the respective substituted alanine analogues of alloferon 1. The CuH-1L, CuH-2L and CuH-3L complexes of the tryptophan analogues are more stable from 1 to 5 log units in comparison to those of the alanine analogues. This stabilization of the complexes may result from cation(Cu(II))-π and indole/imidazole ring interactions. The induction of apoptosis in vivo, in Tenebrio molitor cells by the ligands and their copper(II) complexes at pH7.4 was studied. The biological results show that copper(II) ions in vivo did not cause any apparent apoptotic features. The most active were the H12W peptide and Cu(II)-H12W complex formed at pH7.4.
Cechy publikacji
original-article
Inne
System-identifier
2016CH7989
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