Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents
Blood as connective tissue potentially contains evidence of all processes occurring within the organism, at least in trace amounts (Petricoin et al., 2006) [1]. Because of their small size, peptides penetrate cell membranes and epithelial barriers more freely than proteins. Among the peptides found...
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Language: | English |
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Elsevier
2018-06-01
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Series: | Data in Brief |
Online Access: | http://www.sciencedirect.com/science/article/pii/S235234091830369X |
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doaj-53be858233c14a40b3426079d75b0259 |
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record_format |
Article |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Georgij Arapidi Maria Osetrova Olga Ivanova Ivan Butenko Tatjana Saveleva Polina Pavlovich Nikolay Anikanov Vadim Ivanov Vadim Govorun |
spellingShingle |
Georgij Arapidi Maria Osetrova Olga Ivanova Ivan Butenko Tatjana Saveleva Polina Pavlovich Nikolay Anikanov Vadim Ivanov Vadim Govorun Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents Data in Brief |
author_facet |
Georgij Arapidi Maria Osetrova Olga Ivanova Ivan Butenko Tatjana Saveleva Polina Pavlovich Nikolay Anikanov Vadim Ivanov Vadim Govorun |
author_sort |
Georgij Arapidi |
title |
Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents |
title_short |
Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents |
title_full |
Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents |
title_fullStr |
Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents |
title_full_unstemmed |
Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents |
title_sort |
peptidomics dataset: blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents |
publisher |
Elsevier |
series |
Data in Brief |
issn |
2352-3409 |
publishDate |
2018-06-01 |
description |
Blood as connective tissue potentially contains evidence of all processes occurring within the organism, at least in trace amounts (Petricoin et al., 2006) [1]. Because of their small size, peptides penetrate cell membranes and epithelial barriers more freely than proteins. Among the peptides found in blood, there are both fragments of proteins secreted by various tissues and performing their function in plasma and receptor ligands: hormones, cytokines and mediators of cellular response (Anderson et al., 2002) [2]. In addition, in minor amounts, there are peptide disease markers (for example, oncomarkers) and even foreign peptides related to pathogenic organisms and infection agents. To propose an approach for detailed peptidome characterization, we carried out an LC–MS/MS analysis of blood serum and plasma samples taken from 20 healthy donors on a TripleTOF 5600+ mass-spectrometer. We prepared samples based on our previously developed method of peptide desorption from the surface of abundant blood plasma proteins followed by standard chromatographic steps (Ziganshin et al., 2011) [3]. The mass-spectrometry peptidomics data presented in this article have been deposited to the ProteomeXchange Consortium (Deutsch et al., 2017) [4] via the PRIDE partner repository with the dataset identifier PXD008141 and 10.6019/PXD008141. |
url |
http://www.sciencedirect.com/science/article/pii/S235234091830369X |
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doaj-53be858233c14a40b3426079d75b02592020-11-25T01:12:13ZengElsevierData in Brief2352-34092018-06-011812041211Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbentsGeorgij Arapidi0Maria Osetrova1Olga Ivanova2Ivan Butenko3Tatjana Saveleva4Polina Pavlovich5Nikolay Anikanov6Vadim Ivanov7Vadim Govorun8Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian Federation; Federal Research and Clinical Center of Physical Chemical Medicine of the Federal Medical and Biological Agency of the Russian Federation, Malaya Pirogovskaya 1a, Moscow 119435, Russian Federation; Corresponding author at: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation.Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian FederationMoscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian Federation; Federal Research and Clinical Center of Physical Chemical Medicine of the Federal Medical and Biological Agency of the Russian Federation, Malaya Pirogovskaya 1a, Moscow 119435, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Federal Research and Clinical Center of Physical Chemical Medicine of the Federal Medical and Biological Agency of the Russian Federation, Malaya Pirogovskaya 1a, Moscow 119435, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian Federation; Federal Research and Clinical Center of Physical Chemical Medicine of the Federal Medical and Biological Agency of the Russian Federation, Malaya Pirogovskaya 1a, Moscow 119435, Russian FederationBlood as connective tissue potentially contains evidence of all processes occurring within the organism, at least in trace amounts (Petricoin et al., 2006) [1]. Because of their small size, peptides penetrate cell membranes and epithelial barriers more freely than proteins. Among the peptides found in blood, there are both fragments of proteins secreted by various tissues and performing their function in plasma and receptor ligands: hormones, cytokines and mediators of cellular response (Anderson et al., 2002) [2]. In addition, in minor amounts, there are peptide disease markers (for example, oncomarkers) and even foreign peptides related to pathogenic organisms and infection agents. To propose an approach for detailed peptidome characterization, we carried out an LC–MS/MS analysis of blood serum and plasma samples taken from 20 healthy donors on a TripleTOF 5600+ mass-spectrometer. We prepared samples based on our previously developed method of peptide desorption from the surface of abundant blood plasma proteins followed by standard chromatographic steps (Ziganshin et al., 2011) [3]. The mass-spectrometry peptidomics data presented in this article have been deposited to the ProteomeXchange Consortium (Deutsch et al., 2017) [4] via the PRIDE partner repository with the dataset identifier PXD008141 and 10.6019/PXD008141.http://www.sciencedirect.com/science/article/pii/S235234091830369X |