期刊
PEDIATRIC RESEARCH
卷 57, 期 3, 页码 438-444出版社
NATURE PUBLISHING GROUP
DOI: 10.1203/01.PDR.0000151317.08180.7E
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- NHLBI NIH HHS [HL-61798] Funding Source: Medline
- NICHD NIH HHS [HD-01180, HD-42326] Funding Source: Medline
The human fetus and neonate swallow biologically significant quantities of IL-8/CXC ligand 8 (CXCL8) in amniotic fluid and breast milk, and this remains measurable through simulated neonatal gastric and proximal intestinal digestions. We sought to confirm the structural and functional integrity of IL-8/CXCL8 in digestates and determine the mechanisms underlying this protease resistance. We observed that in comparison with BSA, IL-8/CXCL8 is highly resistant to pepsin and can be detected intact in assays for structural, immunologic, and functional integrity. In a computational molecular docking simulation, IL-8/CXCLS was observed to fit poorly in the pepsin active site. On the basis of simulated mutation analyses, we hypothesized that this protease resistance is due to disulfide bond-related tertiary folding in IL-8/CXCL8. This was confirmed on chemical reduction of these groups.
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