کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1231832 1495263 2013 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Investigation on potential enzyme toxicity of clenbuterol to trypsin
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Investigation on potential enzyme toxicity of clenbuterol to trypsin
چکیده انگلیسی

Clenbuterol (CLB) is a kind of β2-adrenergic agonists which was illegally used as feed additives nowadays. The toxic interaction of CLB with trypsin, an important digestive enzyme, was studied in vitro using multi-spectroscopic methods and molecular modeling methods. CLB was proved to bind with trypsin in S1 pocket, forming a complex driven by the dominant force of H-bond. The binding constant was calculated to be 1.79887 × 105 L mol−1 at 289 K and 0.32584 × 105 L mol−1 at 310 K, respectively. The skeleton of trypsin became loosened and unfolded with the amino residues microenvironment changed. The secondary and tertiary structure of trypsin also varied. Molecular modeling studies illustrated specific display of the binding information and explained most of the experiment phenomena. The binding site of CLB induced the fluorescence quenching as well as inhibition of enzyme activity of trypsin. The study confirmed that CLB had potential toxicity on both the structure and function of trypsin and the effects enhanced with the increasing concentration of CLB.

Figure optionsDownload as PowerPoint slideHighlights
► Interaction mechanism between clenbuterol and trypsin was investigated.
► Multi-spectroscopic methods and molecular modeling methods were applied.
► The structure and function (enzyme activity) of trypsin were both affected by CLB.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 105, 15 March 2013, Pages 200–206
نویسندگان
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