کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5265516 | 1385286 | 2012 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The role of the βAsp residue in copper(II) binding by modified peptides
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The synthesis and binding abilities of peptides containing β-amino acids towards Cu(II) ions are presented. The peptides studied were: Ala-βAsp-Ser-Gly and Arg-Lys-βAsp-Val-Tyr. Potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, CD) in strict correlation with potentiometric measurements. The results obtained on the β-peptides studied allowed the characterization of the influence of this structural modification on the coordination abilities of the peptides. Moreover, the role of the α-Asp position in the peptide chain was also described.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Tetrahedron Letters - Volume 53, Issue 13, 28 March 2012, Pages 1652-1655
Journal: Tetrahedron Letters - Volume 53, Issue 13, 28 March 2012, Pages 1652-1655
نویسندگان
Hanna Czapor-Irzabek, Marek Cebrat, Justyna BrasuÅ,