کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1940758 1050787 2006 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Disulfide bond formation in NGR fiber-modified adenovirus is essential for retargeting to aminopeptidase N
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Disulfide bond formation in NGR fiber-modified adenovirus is essential for retargeting to aminopeptidase N
چکیده انگلیسی

The peptide motif NGR (asparagine–glycine–arginine) is known to bind to aminopepidase N (APN). We have constructed five adenoviruses (Ads) bearing NGR in the HI loop of the adenoviral fiber protein. We compared the targeting properties of the NGR peptide within different amino acid environments and showed that their cellular receptor(s) were not identical. Ads containing NGR within potentially cyclic sequences flanked by cysteines retargeted viruses mainly to APN, while Ads containing NGR within linear sequences not containing cysteines retargeted Ads mainly to αvβ3 integrin, albeit with a lower affinity. Finally, we show evidence that disulfide bond formation within an Ad bearing the CDCNGRCFC sequence is essential for retargeting to APN, suggesting that this sequence does indeed assume a cyclic structure which facilitates NGR binding to APN. Therefore, our study underscores the importance of cysteine residues flanking targeting peptides for not only affinity but also specificity of the retargeted Ad.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 348, Issue 1, 15 September 2006, Pages 278–287
نویسندگان
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