Research ExplorerPublicationsBoronic acid-functionalized mesoporous magnetic particles wi...

Boronic acid-functionalized mesoporous magnetic particles with a hydrophilic surface for the multimodal enrichment of glycopeptides for glycoproteomics

Standard

Boronic acid-functionalized mesoporous magnetic particles with a hydrophilic surface for the multimodal enrichment of glycopeptides for glycoproteomics. / Yang, Lujie; Zhang, Quanqing; Huang, Yuanyu; Lin, Ling; Schlüter, Hartmut; Wang, Ke; Zhang, Cuiping; Yang, Pengyuan; Yu, Hongxiu.

In: ANALYST, Vol. 145, No. 15, 07.08.2020, p. 5252-5259.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Yang, L, Zhang, Q, Huang, Y, Lin, L, Schlüter, H, Wang, K, Zhang, C, Yang, P & Yu, H 2020, 'Boronic acid-functionalized mesoporous magnetic particles with a hydrophilic surface for the multimodal enrichment of glycopeptides for glycoproteomics', ANALYST, vol. 145, no. 15, pp. 5252-5259. https://doi.org/10.1039/d0an00648c

APA

Yang, L., Zhang, Q., Huang, Y., Lin, L., Schlüter, H., Wang, K., Zhang, C., Yang, P., & Yu, H. (2020). Boronic acid-functionalized mesoporous magnetic particles with a hydrophilic surface for the multimodal enrichment of glycopeptides for glycoproteomics. ANALYST, 145(15), 5252-5259. https://doi.org/10.1039/d0an00648c

Vancouver

Yang L, Zhang Q, Huang Y, Lin L, Schlüter H, Wang K et al. Boronic acid-functionalized mesoporous magnetic particles with a hydrophilic surface for the multimodal enrichment of glycopeptides for glycoproteomics. ANALYST. 2020 Aug 7;145(15):5252-5259. https://doi.org/10.1039/d0an00648c

Bibtex

@article{5b83b420c1ff450d908548810c8ef446,
title = "Boronic acid-functionalized mesoporous magnetic particles with a hydrophilic surface for the multimodal enrichment of glycopeptides for glycoproteomics",
abstract = "Glycosylation is an important mechanism of secondary protein processing. Large-scale profiling of glycopeptides released by proteolytic digestion of glycoproteins from biologic samples with complex compositions is limited due to their low abundance. Herein, we present a multimodal material based on boronic acid-modified mesoporous magnetic particles with a hydrophilic surface and enlarged pores around 10 nm. Multimodal enrichment successfully improved the enrichment specificity and efficiency of BMMP by synergistic interaction of hydrophilicity and boronic acid functional groups. The 10 nm pore size allows glycopeptides to enter the channel. Hydrophilic glycopeptides could be selectively enriched with an extremely low limit of detection (0.33 fmol per μL) and a high selectivity (1 : 100). From 2 μL of human serum, 328 unique glycopeptides from 101 glycoproteins were identified. A total of 33% of those glycoproteins overlapped with FDA-cleared blood serum biomarkers. It is expected that BMMP in the future can be used for large-scale biomedical glycoproteomics studies.",
author = "Lujie Yang and Quanqing Zhang and Yuanyu Huang and Ling Lin and Hartmut Schl{\"u}ter and Ke Wang and Cuiping Zhang and Pengyuan Yang and Hongxiu Yu",
year = "2020",
month = aug,
day = "7",
doi = "10.1039/d0an00648c",
language = "English",
volume = "145",
pages = "5252--5259",
journal = "ANALYST",
issn = "0003-2654",
publisher = "ROYAL SOC CHEMISTRY",
number = "15",

}

RIS

TY - JOUR

T1 - Boronic acid-functionalized mesoporous magnetic particles with a hydrophilic surface for the multimodal enrichment of glycopeptides for glycoproteomics

AU - Yang, Lujie

AU - Zhang, Quanqing

AU - Huang, Yuanyu

AU - Lin, Ling

AU - Schlüter, Hartmut

AU - Wang, Ke

AU - Zhang, Cuiping

AU - Yang, Pengyuan

AU - Yu, Hongxiu

PY - 2020/8/7

Y1 - 2020/8/7

N2 - Glycosylation is an important mechanism of secondary protein processing. Large-scale profiling of glycopeptides released by proteolytic digestion of glycoproteins from biologic samples with complex compositions is limited due to their low abundance. Herein, we present a multimodal material based on boronic acid-modified mesoporous magnetic particles with a hydrophilic surface and enlarged pores around 10 nm. Multimodal enrichment successfully improved the enrichment specificity and efficiency of BMMP by synergistic interaction of hydrophilicity and boronic acid functional groups. The 10 nm pore size allows glycopeptides to enter the channel. Hydrophilic glycopeptides could be selectively enriched with an extremely low limit of detection (0.33 fmol per μL) and a high selectivity (1 : 100). From 2 μL of human serum, 328 unique glycopeptides from 101 glycoproteins were identified. A total of 33% of those glycoproteins overlapped with FDA-cleared blood serum biomarkers. It is expected that BMMP in the future can be used for large-scale biomedical glycoproteomics studies.

AB - Glycosylation is an important mechanism of secondary protein processing. Large-scale profiling of glycopeptides released by proteolytic digestion of glycoproteins from biologic samples with complex compositions is limited due to their low abundance. Herein, we present a multimodal material based on boronic acid-modified mesoporous magnetic particles with a hydrophilic surface and enlarged pores around 10 nm. Multimodal enrichment successfully improved the enrichment specificity and efficiency of BMMP by synergistic interaction of hydrophilicity and boronic acid functional groups. The 10 nm pore size allows glycopeptides to enter the channel. Hydrophilic glycopeptides could be selectively enriched with an extremely low limit of detection (0.33 fmol per μL) and a high selectivity (1 : 100). From 2 μL of human serum, 328 unique glycopeptides from 101 glycoproteins were identified. A total of 33% of those glycoproteins overlapped with FDA-cleared blood serum biomarkers. It is expected that BMMP in the future can be used for large-scale biomedical glycoproteomics studies.

U2 - 10.1039/d0an00648c

DO - 10.1039/d0an00648c

M3 - SCORING: Journal article

C2 - 32617538

VL - 145

SP - 5252

EP - 5259

JO - ANALYST

JF - ANALYST

SN - 0003-2654

IS - 15

ER -