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(苯并脲基)磺酰胺基受体部分的受控锚固:结合部位倍增对络合性质的影响。

Controlled Anchoring of (Phenylureido)sulfonamide-Based Receptor Moieties: An Impact of Binding Site Multiplication on Complexation Properties.

机构信息

Institute of Chemical Process Fundamentals of CAS, v.v.i., Rozvojová 135, 16502 Prague 6, Czech Republic.

Department of Solid State Chemistry, University of Chemistry and Technology Prague, Technická 5, 16828 Prague 6, Czech Republic.

出版信息

Molecules. 2021 Sep 18;26(18):5670. doi: 10.3390/molecules26185670.

DOI:10.3390/molecules26185670
PMID:34577148
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8468139/
Abstract

The repetition of urea-based binding units within the receptor structure does not only lead to monomer properties multiplication. As confirmed by spectroscopic studies, UV-Vis and H-NMR in classical or competitive titration mode, the attachment to a carrier allocates the active moieties to mutual positions predetermining the function of the whole receptor molecule. Bivalent receptors form self-aggregates. Dendritic receptors with low dihydrogen phosphate loadings offer a cooperative complexation mode associated with a positive dendritic effect. In higher dihydrogen phosphate concentrations, the dendritic branches act independently and the binding mode changes to 1:1 anion: complexation site. Despite the anchoring, the dendritic receptors retain the superior efficiency and selectivity of a monomer, paving the way to recyclable receptors, desirable for economic and ecological reasons.

摘要

在受体结构内重复的脲基结合单元不仅导致单体性质的倍增。正如光谱研究、经典或竞争滴定模式中的 UV-Vis 和 H-NMR 所证实的那样,与载体的附着将活性部分分配到相互位置,预先确定整个受体分子的功能。二价受体形成自聚集物。具有低二氢磷酸盐负载的树枝状受体提供与正树枝状效应相关的协同络合模式。在较高的二氢磷酸盐浓度下,树枝状分支独立作用,结合模式变为 1:1 阴离子:络合位点。尽管有锚固作用,但树枝状受体仍保持单体的优异效率和选择性,为经济和生态原因开辟了可回收受体的道路。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/7ad76d9e110a/molecules-26-05670-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/aa6782a353c1/molecules-26-05670-sch001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/a5ab64072605/molecules-26-05670-sch002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/f064bd62d96b/molecules-26-05670-sch003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/6d92f9fe135d/molecules-26-05670-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/7ad76d9e110a/molecules-26-05670-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/aa6782a353c1/molecules-26-05670-sch001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/a5ab64072605/molecules-26-05670-sch002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/f064bd62d96b/molecules-26-05670-sch003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/6d92f9fe135d/molecules-26-05670-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0ed3/8468139/7ad76d9e110a/molecules-26-05670-g002.jpg

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