کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2008458 1066415 2007 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Novel analogs of VIP with multiple C-terminal domains
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Novel analogs of VIP with multiple C-terminal domains
چکیده انگلیسی

The effect of multiplication of the N-terminal domain of vasoactive intestinal peptide (VIP) on the binding activity of the peptide was recently evaluated. A VIP analog with multiple N-terminal domains was found to be slightly more potent as compared to [Nle17]VIP towards VIP receptor type 1 (VPAC1)—related cAMP production. Here, the effect of multiplication of the C-terminal domain of VIP was evaluated with the aim of possibly amplifying peptide-receptor (VPAC1) binding and activation. Several VIP analogs were designed and synthesized, each carrying multiplication of the C-terminal domain that was obtained by either a simple linear tandem extension or by a unique branching methodology. Results show that despite significant alterations in the C-terminal domain of VIP that is considered essential to induce potent receptor binding, few peptides demonstrated only slight reduction in receptor binding and activation in comparison to [Nle17]VIP. Furthermore, a specific branched VIP analog with multiple C-terminal domains was equipotent to [Nle17]VIP in the cAMP production assay. Therefore, it is concluded that the association between the VIP ligand to the VIP receptor could be tolerable to size increases in the C-terminal region of the VIP ligand and multiplication of the C-terminal does not increase activity.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Peptides - Volume 28, Issue 9, September 2007, Pages 1622–1630
نویسندگان
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