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通过类似李息岗的酶辅助机制,从连续的到小球形肽组装体的转变。

Transition from continuous to microglobular shaped peptide assemblies through a Liesegang-like enzyme-assisted mechanism.

机构信息

Université de Strasbourg, CNRS, Institut Charles Sadron UPR 22, 67034 Strasbourg, France; Institut National de la Santé et de la Recherche Médicale, UMR-S 1121, "Biomatériaux et Bioingénierie", 67084 Strasbourg, France; Université de Strasbourg, Faculté de Chirurgie Dentaire, Fédération de Médecine Translationnelle de Strasbourg (FMTS), and Fédération des Matériaux et Nanoscience d'Alsace (FMNA), 67000 Strasbourg, France.

Université de Nantes, ONIRIS, INSERM UMR 1229, 1 place Alexis Ricordeau, 44042 Nantes, France.

出版信息

J Colloid Interface Sci. 2023 Mar;633:876-885. doi: 10.1016/j.jcis.2022.11.034. Epub 2022 Nov 18.

DOI:10.1016/j.jcis.2022.11.034
PMID:36495809
Abstract

Enzyme-assisted self-assembly confined within host materials leads to Liesegang-like spatial structuration when precursor peptides are diffusing through an enzyme-functionalized hydrogel. It is shown here that playing on peptide and enzyme concentrations results in a transition from continuous self-assembled peptide areas to individual microglobules. Their morphology, location, size and buildup mechanism are described. Additionally, it is also found that the enzymes adsorb onto the peptide self-assemblies leading to co-localization of peptide self-assembled microglobules and enzymes. Finally, we find that large microglobules grow at the expense of smaller ones present in their vicinity in a kind of Ostwald ripening process, illustrating the dynamic nature of the peptide self-assembly process within host hydrogels.

摘要

当前体肽扩散通过酶功能化水凝胶时,酶辅助的自组装被限制在主体材料内,导致类似李息格的空间结构化。这里表明,通过控制肽和酶的浓度,可以实现从连续的自组装肽区域到单个微球的转变。描述了它们的形态、位置、大小和形成机制。此外,还发现酶吸附在肽自组装上,导致肽自组装微球和酶的共定位。最后,我们发现大微球在其附近的小微球的消耗下生长,形成一种奥斯特瓦尔德熟化过程,说明了在主体水凝胶中肽自组装过程的动态性质。

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