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Removal of SDS from biological protein digests for proteomic analysis by mass spectrometry

Overview of attention for article published in Proteome Science, September 2016
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Title
Removal of SDS from biological protein digests for proteomic analysis by mass spectrometry
Published in
Proteome Science, September 2016
DOI 10.1186/s12953-016-0098-5
Pubmed ID
Authors

Soundharrajan Ilavenil, Naif Abdullah Al-Dhabi, Srisesharam Srigopalram, Young Ock Kim, Paul Agastian, Rajasekhar Baaru, Ki Choon Choi, Mariadhas Valan Arasu, Chun Geon Park, Kyung Hun Park

Abstract

Metal-organic frameworks (MOFs - MIL-101) are the most exciting, high profiled developments in nanotechnology in the last ten years, and it attracted considerable attention owing to their uniform nanoporosity, large surface area, outer-surface modification and in-pore functionality for tailoring the chemical properties of the material for anchoring specific guest moieties. MOF's have been particularly highlighted for their excellent gas storage and separation properties. Recently biomolecules-based MOF's were used as nanoencapsulators for antitumor and antiretroviral controlled drug delivery studies. However, usage of MOF material for removal of ionic detergent-SDS from biological samples has not been reported to date. Here, first time we demonstrate its novel applications in biological sample preparation for mass spectrometry analysis. SDS removal using MIL-101 was assessed for proteomic analysis by mass spectrometry. We analysed removal of SDS from 0.5 % SDS solution alone, BSA mixture and HMEC cells lysate protein mixture. The removal of SDS by MIL-101 was confirmed by MALDI-TOF-MS and LC-MS techniques. In an initial demonstration, SDS has removed effectively from 0.5 % SDS solution by MIL-101via its binding attraction with SDS. Further, the experiment also confirmed that MIL-101 strongly removed the SDS from BSA and cell lysate mixtures. These results suggest that SDS removal by the MIL-101 method is a practical, simple and broad applicable in proteomic sample processing for MALDI-TOF-MS and LC-MS analysis.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 39 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 39 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 7 18%
Researcher 7 18%
Student > Bachelor 6 15%
Student > Master 3 8%
Other 2 5%
Other 4 10%
Unknown 10 26%
Readers by discipline Count As %
Chemistry 8 21%
Biochemistry, Genetics and Molecular Biology 8 21%
Pharmacology, Toxicology and Pharmaceutical Science 4 10%
Agricultural and Biological Sciences 3 8%
Veterinary Science and Veterinary Medicine 1 3%
Other 3 8%
Unknown 12 31%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 September 2016.
All research outputs
#20,340,423
of 22,886,568 outputs
Outputs from Proteome Science
#159
of 192 outputs
Outputs of similar age
#291,904
of 334,695 outputs
Outputs of similar age from Proteome Science
#3
of 3 outputs
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So far Altmetric has tracked 192 research outputs from this source. They receive a mean Attention Score of 2.7. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
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