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Updated: Jan 31, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
Published on: November 18, 2014
Protein and peptide profiles in neonatal meconium
Barbara Lisowska-Myjak1, Ewa Skarżyńska1, Konrad Wojdan2
1Department of Biochemistry and Clinical Chemistry, Medical University of Warsaw, Warsaw, Poland.
Aim:
The proteins accumulated in the meconium reflect the intrauterine environment and are naturally excreted by a neonate. The identification and classification of individual meconium proteins may be a valuable source of information about physiological and pathological processes in utero.
Methods:
Proteomic analysis was used to study the protein composition in pooled 50 serial meconium portions from 10 neonates. The proteins were classified based on the gene ontology database. The amounts and relative number of proteins (%) in the identified categories and their subcategories were assessed.
Results:
A total of 946 proteins identified in meconium, including 430 represented by two or more peptides were classified into three categories: biological process (n = 401), molecular function (n = 386) and cellular component (n = 422). The highest number of proteins (>25% of the total) was found in the subcategories: developmental processes, signaling, transport, response to stimulus, regulation, metabolic processes, ion binding, extracellular region, membrane and cytoplasm.
Conclusion:
The composition of meconium proteins identified in this study may be a rich source of new biomarkers for use in neonatology with a potential to predict later development.
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