【摘 要】
：
In general,small peptide sequences taken from proteins do not display a particular fold on the basis of their primary amino acid sequence and are therefore
【机 构】
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RadboudUniversityNijmegenTheNetherlands
【出 处】
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2008中国深圳蛋白质和多肽科学大会
论文部分内容阅读
In general,small peptide sequences taken from proteins do not display a particular fold on the basis of their primary amino acid sequence and are therefore often biologically inactive.It is the rest of the protein that positions the peptide in space and provides secondary structural integrity.Therefore,a lot of research has focussed on restoring this native fold and hence the activity of these small peptides.Recently,we have demonstrated that it is possible to display a peptide on a liposome surface and,more importantly,to stabilize it in its native fold,by the attachment of hydrophobic anchors to both the N-and C-terminus,in order to produce a biologically active species.Now,we want exploit this strategy to try to manipulate and switch the conformation of peptides to control their biological activity.
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