کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2007870 1066388 2007 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structure–function studies of peptides for cell adhesion inhibition: Identification of key residues by alanine mutation and peptide-truncation approach
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Structure–function studies of peptides for cell adhesion inhibition: Identification of key residues by alanine mutation and peptide-truncation approach
چکیده انگلیسی

Blockage of the interaction of CD2 with its ligand CD58 is expected to bring out potential therapeutic value for autoimmune diseases and organ transplantation. Three series of peptides (cVL, cIL and cAQ series) were designed from ratCD2 and humanCD2 to modulate CD2–CD58 interaction. To determine the specific segments in parent peptides responsible for inhibitory activity as lead sequence, we generated shorter fragments of the parent peptides and evaluated their biological activity with cell adhesion assay. The structure–activity relationship studies indicated that small cyclic peptides derived from CD2 ligand binding epitopes could mimic native β-turn structure, and thus modulate CD2–CD58 interaction.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Peptides - Volume 28, Issue 8, August 2007, Pages 1498–1508
نویسندگان
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