کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1941608 1536901 2016 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Probing the polarity and water environment at the protein-peptide binding interface using tryptophan analogues
ترجمه فارسی عنوان
کاوش قطبیت و محیط آب در رابط اتصال دهنده پروتئین ـ پپتید با استفاده از آنالوگ های تریپتوفان
کلمات کلیدی
کالمدولین؛ پپتید اتصال دهنده Calmodulin؛ آنالوگهای تریپتوفان غیر طبیعی؛
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
چکیده انگلیسی


• Probe calmodulin-peptide interaction by tryptophan analogues incorporated peptides.
• These peptides are sensitive to polarity and water contents at the binding interface.
• Significant luminescence changes deduce the binding constant and interface property.

7-Azatryptophan and 2,7-diazatryptophan are sensitive to polarity changes and water content, respectively, and should be ideal for studying protein-protein and protein-peptide interactions. In this study, we replaced the tryptophan in peptide Baa (LKWKKLLKLLKKLLKLG-NH2) with 7-azatryptophan or 2,7-diazatryptophan, forming (7-aza)Trp-Baa and (2,7-aza)Trp-Baa, to study the calmodulin (CaM)-peptide interaction. Dramatic differences in the (7-aza)Trp-Baa and (2,7-aza)Trp-Baa fluorescence properties between free peptide in water and calmodulin-bound peptide were observed, showing a less polar and water scant environment at the binding interface of the peptide upon calmodulin binding. The affinity of the peptides for binding CaM followed the trend Baa (210±10 pM)<(7-aza)Trp-Baa (109±5 pM)<(2,7-aza)Trp-Baa (45±2 pM), showing moderate increase in binding affinity upon increasing the number of nitrogen atoms in the Trp analogue. The increased binding affinity may be due to the formation of more hydrogen bonds upon binding CaM for the Trp analogue with more nitrogen atoms. Importantly, the results demonstrate that (7-aza)Trp and (2,7-aza)Trp are excellent probes for exploring the environment at the interface of protein-peptide interactions.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemistry and Biophysics Reports - Volume 7, September 2016, Pages 113–118
نویسندگان
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