Sofia Guedes, Luís Perpétuo, Jacinta Veloso, Tânia Lima, Ana F Ferreira, Inês Pires, Francisca Savaiva, André Lourenço, Liliana Moreira-Costa, Adelino Leite-Moreira, Antonio Barros, Fábio Trindade, Rui Vitorino
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We also took advantage of recent advances in DBS mass spectrometry to ensure accurate detection and quantification.</p><p><strong>Results: </strong>A comprehensive analysis identified 972 modified peptides in DBS samples. Of these, a subset of 211 peptides was consistently present in all samples, highlighting their potential biological importance and relevance. This indicates a diverse spectrum of PTMs in the proteome of DBS samples.</p><p><strong>Conclusions and clinical relevance: </strong>Integration of mass spectrometry and proteomics has revealed a broad spectrum of modified peptides in DBS samples and highlighted their importance in biological processes and disease progression. Accurate detection of these PTMs may be critical for risk stratification and disease management. This study improves the understanding of molecular mechanisms underlying biological processes and disease development, providing important insights for clinical applications.</p>","PeriodicalId":20571,"journal":{"name":"PROTEOMICS – Clinical Applications","volume":" ","pages":"e2300102"},"PeriodicalIF":2.1000,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Comprehensive characterization of protein modifications using mass spectrometry and dry blood spots.\",\"authors\":\"Sofia Guedes, Luís Perpétuo, Jacinta Veloso, Tânia Lima, Ana F Ferreira, Inês Pires, Francisca Savaiva, André Lourenço, Liliana Moreira-Costa, Adelino Leite-Moreira, Antonio Barros, Fábio Trindade, Rui Vitorino\",\"doi\":\"10.1002/prca.202300102\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><strong>Purpose: </strong>The main objective of this study is to characterize and analyze modified peptides in DBS samples. This includes deciphering their specific PTMs and understanding their potential impact on the population or disease cohort under study.</p><p><strong>Experimental design: </strong>Using mass spectrometry-based proteomic approaches, we performed a comprehensive analysis of DBS samples. Our focus was on the identification and quantification of modified peptides. We also took advantage of recent advances in DBS mass spectrometry to ensure accurate detection and quantification.</p><p><strong>Results: </strong>A comprehensive analysis identified 972 modified peptides in DBS samples. Of these, a subset of 211 peptides was consistently present in all samples, highlighting their potential biological importance and relevance. This indicates a diverse spectrum of PTMs in the proteome of DBS samples.</p><p><strong>Conclusions and clinical relevance: </strong>Integration of mass spectrometry and proteomics has revealed a broad spectrum of modified peptides in DBS samples and highlighted their importance in biological processes and disease progression. Accurate detection of these PTMs may be critical for risk stratification and disease management. This study improves the understanding of molecular mechanisms underlying biological processes and disease development, providing important insights for clinical applications.</p>\",\"PeriodicalId\":20571,\"journal\":{\"name\":\"PROTEOMICS – Clinical Applications\",\"volume\":\" \",\"pages\":\"e2300102\"},\"PeriodicalIF\":2.1000,\"publicationDate\":\"2024-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"PROTEOMICS – Clinical Applications\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1002/prca.202300102\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/1/2 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"PROTEOMICS – Clinical Applications","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1002/prca.202300102","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/1/2 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
Comprehensive characterization of protein modifications using mass spectrometry and dry blood spots.
Purpose: The main objective of this study is to characterize and analyze modified peptides in DBS samples. This includes deciphering their specific PTMs and understanding their potential impact on the population or disease cohort under study.
Experimental design: Using mass spectrometry-based proteomic approaches, we performed a comprehensive analysis of DBS samples. Our focus was on the identification and quantification of modified peptides. We also took advantage of recent advances in DBS mass spectrometry to ensure accurate detection and quantification.
Results: A comprehensive analysis identified 972 modified peptides in DBS samples. Of these, a subset of 211 peptides was consistently present in all samples, highlighting their potential biological importance and relevance. This indicates a diverse spectrum of PTMs in the proteome of DBS samples.
Conclusions and clinical relevance: Integration of mass spectrometry and proteomics has revealed a broad spectrum of modified peptides in DBS samples and highlighted their importance in biological processes and disease progression. Accurate detection of these PTMs may be critical for risk stratification and disease management. This study improves the understanding of molecular mechanisms underlying biological processes and disease development, providing important insights for clinical applications.
期刊介绍:
PROTEOMICS - Clinical Applications has developed into a key source of information in the field of applying proteomics to the study of human disease and translation to the clinic. With 12 issues per year, the journal will publish papers in all relevant areas including:
-basic proteomic research designed to further understand the molecular mechanisms underlying dysfunction in human disease
-the results of proteomic studies dedicated to the discovery and validation of diagnostic and prognostic disease biomarkers
-the use of proteomics for the discovery of novel drug targets
-the application of proteomics in the drug development pipeline
-the use of proteomics as a component of clinical trials.