Improved breast milk proteome coverage by DIA based LC‐MS/MS method
The breast milk composition includes a multitude of bioactive factors such as viable cells, lipids and proteins. Measuring the levels of specific proteins in breast milk plasma can be challenging because of the large dynamic range of protein concentrations and the presence of interfering substances....
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| Veröffentlicht in: | Proteomics (Weinheim) 2024-07, Vol.24 (14), p.e2300340-n/a |
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| creator | Viitaharju, Jenni Polari, Lauri Kauko, Otto Merilahti, Johannes Rokka, Anne Toivola, Diana M. Laitinen, Kirsi |
| description | The breast milk composition includes a multitude of bioactive factors such as viable cells, lipids and proteins. Measuring the levels of specific proteins in breast milk plasma can be challenging because of the large dynamic range of protein concentrations and the presence of interfering substances. Therefore, most proteomic studies of breast milk have been able to identify under 1000 proteins. Optimised procedures and the latest separation technologies used in milk proteome research could lead to more precise knowledge of breast milk proteome. This study (n = 53) utilizes three different protein quantification methods, including direct DIA, library‐based DIA method and a hybrid method combining direct DIA and library‐based DIA. On average we identified 2400 proteins by hybrid method. By applying these methods, we quantified body mass index (BMI) associated variation in breast milk proteomes. There were 210 significantly different proteins when comparing the breast milk proteome of obese and overweight mothers. In addition, we analysed a small cohort (n = 5, randomly selected from 53 samples) by high field asymmetric waveform ion mobility spectrometry (FAIMS). FAIMS coupled with the Orbitrap Fusion Lumos mass spectrometer, which led to 41.7% higher number of protein identifications compared to Q Exactive HF mass spectrometer. |
| doi_str_mv | 10.1002/pmic.202300340 |
| format | Article |
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Measuring the levels of specific proteins in breast milk plasma can be challenging because of the large dynamic range of protein concentrations and the presence of interfering substances. Therefore, most proteomic studies of breast milk have been able to identify under 1000 proteins. Optimised procedures and the latest separation technologies used in milk proteome research could lead to more precise knowledge of breast milk proteome. This study (n = 53) utilizes three different protein quantification methods, including direct DIA, library‐based DIA method and a hybrid method combining direct DIA and library‐based DIA. On average we identified 2400 proteins by hybrid method. By applying these methods, we quantified body mass index (BMI) associated variation in breast milk proteomes. There were 210 significantly different proteins when comparing the breast milk proteome of obese and overweight mothers. In addition, we analysed a small cohort (n = 5, randomly selected from 53 samples) by high field asymmetric waveform ion mobility spectrometry (FAIMS). 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Measuring the levels of specific proteins in breast milk plasma can be challenging because of the large dynamic range of protein concentrations and the presence of interfering substances. Therefore, most proteomic studies of breast milk have been able to identify under 1000 proteins. Optimised procedures and the latest separation technologies used in milk proteome research could lead to more precise knowledge of breast milk proteome. This study (n = 53) utilizes three different protein quantification methods, including direct DIA, library‐based DIA method and a hybrid method combining direct DIA and library‐based DIA. On average we identified 2400 proteins by hybrid method. By applying these methods, we quantified body mass index (BMI) associated variation in breast milk proteomes. There were 210 significantly different proteins when comparing the breast milk proteome of obese and overweight mothers. In addition, we analysed a small cohort (n = 5, randomly selected from 53 samples) by high field asymmetric waveform ion mobility spectrometry (FAIMS). FAIMS coupled with the Orbitrap Fusion Lumos mass spectrometer, which led to 41.7% higher number of protein identifications compared to Q Exactive HF mass spectrometer.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>38873899</pmid><doi>10.1002/pmic.202300340</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0001-8272-3939</orcidid><orcidid>https://orcid.org/0000-0001-5245-8118</orcidid><orcidid>https://orcid.org/0000-0003-1482-9154</orcidid><orcidid>https://orcid.org/0000-0002-9113-5175</orcidid><orcidid>https://orcid.org/0000-0001-7165-9839</orcidid><orcidid>https://orcid.org/0000-0002-0052-6489</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adult Body mass index Body size Breast milk Breastfeeding & lactation Chromatography, Liquid - methods colostrum Female Fusion protein Humans Ion Mobility Spectrometry - methods Ionic mobility Libraries Lipids Liquid Chromatography-Mass Spectrometry Mass spectrometers mass spectrometry Milk Proteins - analysis Milk, Human - chemistry obesity Protein composition Proteins Proteome - analysis Proteomes Proteomics Proteomics - methods Spectrometry Tandem Mass Spectrometry - methods Waveforms |
| title | Improved breast milk proteome coverage by DIA based LC‐MS/MS method |
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