ArticleRapid communications in mass spectrometry : RCM2025
Characterization of N-Terminal Acetylated α-Hemoglobin Stabilizing Protein (AHSP) by Top-Down High-Resolution Mass Spectrometry From Human Preterm Newborns Oral Fluid.
Article in Rapid communications in mass spectrometry : RCM, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Characterization of N-Terminal Acetylated α-Hemoglobin Stabilizing Protein (AHSP) by Top-Down High-Resolution Mass Spectrometry From Human Preterm Newborns Oral Fluid.Rapid communications in mass spectrometry : RCM · 2025Article
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20 authors.
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Abstract
rationaleAlpha-hemoglobin stabilizing protein (AHSP) is an erythroid-specific protein forming a stable complex with free α-hemoglobin, but not with β-hemoglobin or hemoglobin A (α
methodsThe primary structure of AHSP was determined by high-resolution top-down proteomic analysis using a nano-HPLC-ESI-MS/MS approach on oral fluid samples from preterm newborns. Specimens were collected non-invasively from infants, promptly treated with formic acid, and analyzed with an Orbitrap-based mass spectrometry platform. The intact protein's molecular mass and fragmentation pattern were assessed to determine its primary structure and post-translational modifications. Statistical analysis was performed to explore correlations between AHSP presence and neonatal clinical parameters, including anemia and transfusion needs.
resultsThe experimental monoisotopic molecular mass value [M + H
conclusionsAlthough the data obtained so far cannot be used for quantitative analysis or statistical evaluation, AHSP appears to stand out as a potential early biomarker of neonatal hematological disorders, highlighting a new perspective for future investigations.
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