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Preparation of protein imprinted materials by hierarchical imprinting techniques and application in selective depletion of albumin from human serum

Hierarchical imprinting was developed to prepare the protein imprinted materials, as the artificial antibody, for the selective depletion of HSA from the human serum proteome. Porcine serum albumin (PSA) was employed as the dummy template for the fabrication of the recognition sites. To demonstrate...

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Autores principales: Liu, Jinxiang, Deng, Qiliang, Tao, Dingyin, Yang, Kaiguang, Zhang, Lihua, Liang, Zhen, Zhang, Yukui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4074782/
https://www.ncbi.nlm.nih.gov/pubmed/24976158
http://dx.doi.org/10.1038/srep05487
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author Liu, Jinxiang
Deng, Qiliang
Tao, Dingyin
Yang, Kaiguang
Zhang, Lihua
Liang, Zhen
Zhang, Yukui
author_facet Liu, Jinxiang
Deng, Qiliang
Tao, Dingyin
Yang, Kaiguang
Zhang, Lihua
Liang, Zhen
Zhang, Yukui
author_sort Liu, Jinxiang
collection PubMed
description Hierarchical imprinting was developed to prepare the protein imprinted materials, as the artificial antibody, for the selective depletion of HSA from the human serum proteome. Porcine serum albumin (PSA) was employed as the dummy template for the fabrication of the recognition sites. To demonstrate the advantages of the hierarchical imprinting, molecularly imprinted polymers prepared by hierarchical imprinting technique (h-MIPs) were compared with those obtained by bulk imprinting (b-MIPs), in terms of the binding capacity, adsorption kinetics, selectivity and synthesis reproducibility. The binding capacity of h-MIPs could reach 12 mg g(−1). And saturation binding could be reached in less than 20 min for the h-MIPs. In the protein mixture, h-MIPs exhibit excellent selectivity for PSA, with imprinting factors as about 3.6, much higher than those for non-template proteins. For the proteomic application, the identified protein group number in serum treated by h-MIPs was increased to 422, which is 21% higher than that obtained from the original serum, meanwhile the identified protein group number for the Albumin Removal kit was only 376. The results demonstrate that protein imprinted polymers prepared by hierarchical imprinting technique, might become the artificial antibodies for the selective depletion of high abundance proteins in proteome study.
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spelling pubmed-40747822014-07-01 Preparation of protein imprinted materials by hierarchical imprinting techniques and application in selective depletion of albumin from human serum Liu, Jinxiang Deng, Qiliang Tao, Dingyin Yang, Kaiguang Zhang, Lihua Liang, Zhen Zhang, Yukui Sci Rep Article Hierarchical imprinting was developed to prepare the protein imprinted materials, as the artificial antibody, for the selective depletion of HSA from the human serum proteome. Porcine serum albumin (PSA) was employed as the dummy template for the fabrication of the recognition sites. To demonstrate the advantages of the hierarchical imprinting, molecularly imprinted polymers prepared by hierarchical imprinting technique (h-MIPs) were compared with those obtained by bulk imprinting (b-MIPs), in terms of the binding capacity, adsorption kinetics, selectivity and synthesis reproducibility. The binding capacity of h-MIPs could reach 12 mg g(−1). And saturation binding could be reached in less than 20 min for the h-MIPs. In the protein mixture, h-MIPs exhibit excellent selectivity for PSA, with imprinting factors as about 3.6, much higher than those for non-template proteins. For the proteomic application, the identified protein group number in serum treated by h-MIPs was increased to 422, which is 21% higher than that obtained from the original serum, meanwhile the identified protein group number for the Albumin Removal kit was only 376. The results demonstrate that protein imprinted polymers prepared by hierarchical imprinting technique, might become the artificial antibodies for the selective depletion of high abundance proteins in proteome study. Nature Publishing Group 2014-06-30 /pmc/articles/PMC4074782/ /pubmed/24976158 http://dx.doi.org/10.1038/srep05487 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/4.0/
spellingShingle Article
Liu, Jinxiang
Deng, Qiliang
Tao, Dingyin
Yang, Kaiguang
Zhang, Lihua
Liang, Zhen
Zhang, Yukui
Preparation of protein imprinted materials by hierarchical imprinting techniques and application in selective depletion of albumin from human serum
title Preparation of protein imprinted materials by hierarchical imprinting techniques and application in selective depletion of albumin from human serum
title_full Preparation of protein imprinted materials by hierarchical imprinting techniques and application in selective depletion of albumin from human serum
title_fullStr Preparation of protein imprinted materials by hierarchical imprinting techniques and application in selective depletion of albumin from human serum
title_full_unstemmed Preparation of protein imprinted materials by hierarchical imprinting techniques and application in selective depletion of albumin from human serum
title_short Preparation of protein imprinted materials by hierarchical imprinting techniques and application in selective depletion of albumin from human serum
title_sort preparation of protein imprinted materials by hierarchical imprinting techniques and application in selective depletion of albumin from human serum
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4074782/
https://www.ncbi.nlm.nih.gov/pubmed/24976158
http://dx.doi.org/10.1038/srep05487
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