کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1316170 | 976431 | 2010 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cu(II) ion interaction with teicoplanin-vancomycin's analog
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی معدنی
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چکیده انگلیسی
Teicoplanin, a member of the “last chance” antibiotic family has a similar structure and the same mechanism of action as parent drug vancomycin, which is proved to be an effective binder of Cu(II) ions. However, the potentiometric and spectroscopic studies (UV-visible, CD, NMR) have shown that the modification of the N-terminal structure of the peptide backbone in teicoplanin affects considerably the binding ability towards Cu(II) ions. While vancomycin forms almost instantly the stable 3Â N complex species involving the N-terminal and two amide nitrogen donors, in case of teicoplanin only two nitrogen donors derived from the N-terminal amino group and adjacent peptide bond are coordinated to Cu(II) ion within the whole pH range studied. The major factor influencing the binding mode is most likely the structure of the N-terminus of the peptide unit in the antibiotic ligand.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Inorganic Biochemistry - Volume 104, Issue 2, February 2010, Pages 193-198
Journal: Journal of Inorganic Biochemistry - Volume 104, Issue 2, February 2010, Pages 193-198
نویسندگان
Magdalena Brzezowska, Marzena Kucharczyk-KlamiÅska, Francesca Bernardi, Daniela Valensin, Nicola Gaggelli, Elena Gaggelli, Gianni Valensin, MaÅgorzata Jeżowska-Bojczuk,