【摘 要】
：
Thiol-disulfide exchanges are dynamic reactions that widely exist in organisms.Complex thiol-disulfide exchanges can take place on the cell surface due to the presence of many kinds of thiol-/disulfid
【机 构】
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College of Chemistry and Chemical Engineering,The MOE Key Laboratory of Spectrochemical Analysis and
【出 处】
：
2016年分析化学前沿国际研讨会及中美分析化学研讨会
论文部分内容阅读
Thiol-disulfide exchanges are dynamic reactions that widely exist in organisms.Complex thiol-disulfide exchanges can take place on the cell surface due to the presence of many kinds of thiol-/disulfide-containing proteins.It has been reported that the thiol-disulfide exchanges can enhance the efficiency of cellular uptake of various materials bearing thiol-reactive groups.When peptides containing different number of cysteine residues interact with cells,thiol-disulfide exchanges might also influence their cellular uptake.Particularly,these exchange reactions might become complicated if the cysteine residues in peptides are arranged specifically.Here,we designed a series of peptide probes containing a "CXnC"(n = 0,1,2)motif.Disulfide bonds with different kinds of steric hindrance can be formed after oxidation.We examined the thiol-disulfide exchange reactions between peptides and cell surface,and evaluated the intracellular uptake of these oxidized peptides(Fig.1).We further ranked these thiol-disulfide exchanges and divided them into several groups.Control experiments including blocking thiols on the cell surface through disulfide formation and reducing exofacial disulfides into thiols,also confirmed the proposed mechanism describing the dynamic disulfide exchange reactions on cell surface.On this basis we obtained an optimal CXC motif that can be inserted into various peptides to enhance their intracellular delivery.
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