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Peptide Characterization and Functional Stability of a Partially Hydrolyzed Whey-Based Formula over Time
Human clinical trials have shown that a specific partially hydrolyzed 100% whey-based infant formula (pHF-W) reduces AD risk in the first yeast of life. Meta-analyses with a specific pHF-W (pHF-W1) confirm a protective effect while other meta-analyses pooling different pHF-W show conflicting results...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8465316/ https://www.ncbi.nlm.nih.gov/pubmed/34578889 http://dx.doi.org/10.3390/nu13093011 |
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author | Bourdeau, Tristan Affolter, Michael Dupuis, Lénaïck Panchaud, Alexandre Lahrichi, Sabine Merminod, Loraine Martin-Paschoud, Christine Adams, Rachel Nutten, Sophie Blanchard, Carine |
author_facet | Bourdeau, Tristan Affolter, Michael Dupuis, Lénaïck Panchaud, Alexandre Lahrichi, Sabine Merminod, Loraine Martin-Paschoud, Christine Adams, Rachel Nutten, Sophie Blanchard, Carine |
author_sort | Bourdeau, Tristan |
collection | PubMed |
description | Human clinical trials have shown that a specific partially hydrolyzed 100% whey-based infant formula (pHF-W) reduces AD risk in the first yeast of life. Meta-analyses with a specific pHF-W (pHF-W1) confirm a protective effect while other meta-analyses pooling different pHF-W show conflicting results. Here we investigated the molecular composition and functional properties of the specific pHF-W1 as well as the stability of its manufacturing process over time. This specific pHF-W1 was compared with other pHF-Ws. We used size exclusion chromatography to characterize the peptide molecular weight (MW), a rat basophil degranulation assay to assess the relative level of beta-lactoglobulin (BLG) allergenicity and a preclinical model of oral tolerance induction to test prevention of allergic sensitization. To analyze the exact peptide sequences before and after an HLA binding assay, a mass cytometry approach was used. Peptide size allergenicity and oral tolerance induction were conserved across pHF-W1 batches of production and time. The median MW of the 37 samples of pHF-W1 tested was 800 ± 400 Da. Further oral tolerance induction was observed using 10 different batches of the pHF-W1 with a mean reduction of BLG-specific IgE levels of 0.76 log (95% CI = −0.95; −0.57). When comparing pHF-W1 with three other formulas (pHF-W2 3 and 4), peptide size was not necessarily associated with allergenicity reduction in vitro nor oral tolerance induction in vivo as measured by specific IgE level (p < 0.05 for pHF-W1 and 2 and p = 0.271 and p = 0.189 for pHF-W3 and 4 respectively). Peptide composition showed a limited overlap between the formulas tested ranging from 11.7% to 24.2%. Furthermore nine regions in the BLG sequence were identified as binding HLA-DR. In conclusion, not all pHF-Ws tested have the same peptide size distribution decreased allergenicity and ability to induce oral tolerance. Specific peptides are released during the different processes used by different infant formula producers. |
format | Online Article Text |
id | pubmed-8465316 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-84653162021-09-27 Peptide Characterization and Functional Stability of a Partially Hydrolyzed Whey-Based Formula over Time Bourdeau, Tristan Affolter, Michael Dupuis, Lénaïck Panchaud, Alexandre Lahrichi, Sabine Merminod, Loraine Martin-Paschoud, Christine Adams, Rachel Nutten, Sophie Blanchard, Carine Nutrients Article Human clinical trials have shown that a specific partially hydrolyzed 100% whey-based infant formula (pHF-W) reduces AD risk in the first yeast of life. Meta-analyses with a specific pHF-W (pHF-W1) confirm a protective effect while other meta-analyses pooling different pHF-W show conflicting results. Here we investigated the molecular composition and functional properties of the specific pHF-W1 as well as the stability of its manufacturing process over time. This specific pHF-W1 was compared with other pHF-Ws. We used size exclusion chromatography to characterize the peptide molecular weight (MW), a rat basophil degranulation assay to assess the relative level of beta-lactoglobulin (BLG) allergenicity and a preclinical model of oral tolerance induction to test prevention of allergic sensitization. To analyze the exact peptide sequences before and after an HLA binding assay, a mass cytometry approach was used. Peptide size allergenicity and oral tolerance induction were conserved across pHF-W1 batches of production and time. The median MW of the 37 samples of pHF-W1 tested was 800 ± 400 Da. Further oral tolerance induction was observed using 10 different batches of the pHF-W1 with a mean reduction of BLG-specific IgE levels of 0.76 log (95% CI = −0.95; −0.57). When comparing pHF-W1 with three other formulas (pHF-W2 3 and 4), peptide size was not necessarily associated with allergenicity reduction in vitro nor oral tolerance induction in vivo as measured by specific IgE level (p < 0.05 for pHF-W1 and 2 and p = 0.271 and p = 0.189 for pHF-W3 and 4 respectively). Peptide composition showed a limited overlap between the formulas tested ranging from 11.7% to 24.2%. Furthermore nine regions in the BLG sequence were identified as binding HLA-DR. In conclusion, not all pHF-Ws tested have the same peptide size distribution decreased allergenicity and ability to induce oral tolerance. Specific peptides are released during the different processes used by different infant formula producers. MDPI 2021-08-28 /pmc/articles/PMC8465316/ /pubmed/34578889 http://dx.doi.org/10.3390/nu13093011 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Bourdeau, Tristan Affolter, Michael Dupuis, Lénaïck Panchaud, Alexandre Lahrichi, Sabine Merminod, Loraine Martin-Paschoud, Christine Adams, Rachel Nutten, Sophie Blanchard, Carine Peptide Characterization and Functional Stability of a Partially Hydrolyzed Whey-Based Formula over Time |
title | Peptide Characterization and Functional Stability of a Partially Hydrolyzed Whey-Based Formula over Time |
title_full | Peptide Characterization and Functional Stability of a Partially Hydrolyzed Whey-Based Formula over Time |
title_fullStr | Peptide Characterization and Functional Stability of a Partially Hydrolyzed Whey-Based Formula over Time |
title_full_unstemmed | Peptide Characterization and Functional Stability of a Partially Hydrolyzed Whey-Based Formula over Time |
title_short | Peptide Characterization and Functional Stability of a Partially Hydrolyzed Whey-Based Formula over Time |
title_sort | peptide characterization and functional stability of a partially hydrolyzed whey-based formula over time |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8465316/ https://www.ncbi.nlm.nih.gov/pubmed/34578889 http://dx.doi.org/10.3390/nu13093011 |
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