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Improving cell penetration of helical peptides stabilized by N-terminal crosslinked aspartic acids

Org. Biomol. Chem.. 2017-01; 
ZhaoHui, JiangYanhong, TianYuan, YangDan, QinXuan, LiZi
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Biochemicals … image file: c6ob02501c-t2.tif. Theoretical physicochemical parameters. Hydrophobicity (H) was calculated using HeliQuest 23 (effects of FITC were omitted, β-Ala were replaced by Gly). The isoelectric point (IP) was calculated using GenScript Get A Quote

摘要

Cell penetration and nucleus translocation efficiency are important for the cellular activities of peptide therapeutics. For helical peptides stabilized by N-terminal crosslinked aspartic acid, correlations between their penetration efficiency/nucleus translocation and physicochemical properties were studied. An increase in hydrophobicity and isoelectric point will promote cellular uptake and nucleus translocation of stabilized helices.

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