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Internalization of a Peptide into Multilamellar Vesicles Assisted by the Formation of an alpha-Oxo Oxime Bond

机译:肽内化到多层囊泡中,形成α-氧代肟键。

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As part of a drug-delivery project,we designed and synthesised a novel hydroxylamine cholesterol-based anchor to ensure the chemoselective li-gation of recognition patterns onto multilamellar vesicles by oxime liga-tion.The entry of a glyoxylyl peptide into the vesicles was unexpectedly assisted by the formation of the alpha-oxo oxime bond.We studied extensively the kinetic and thermodynamic aspects of this phenomenon.Briefly,for a glyoxylyl peptide,the speed and ability to enter the vesicle were dependent upon 1)the presence of a hydroxylamine anchor of the type Chol-E_3ONH_2,2)the amount of peptide engaged in the ligation and 3)the flip-flop motion permitted by the different formulations,in which the presence of cholesterol seems to play an important role.
机译:作为药物输送项目的一部分,我们设计并合成了一种新型的基于羟胺胆固醇的锚,以确保通过肟连接将识别模式化学选择性连接到多层囊泡上。意外地,乙醛酰肽进入囊泡我们广泛地研究了这种现象的动力学和热力学方面。简而言之,对于乙二醛肽,进入囊泡的速度和能力取决于1)羟胺锚的存在(Chol-E_3ONH_2型),(2)参与连接的肽的量,(3)不同制剂允许的触发运动,其中胆固醇的存在似乎起着重要作用。

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