β-Lactoglobulin detected in human milk forms noncovalent complexes with maltooligosaccharides as revealed by chip-nanoelectrospray high-resolution tandem mass spectrometry

Capitan, Florina; Robu, Adrian C.; Schiopu, Catalin; Ilie, Constantin; Chait, Brian T.; Przybylski, Michael; Zamfir, Alina D.

β-Lactoglobulin detected in human milk forms noncovalent complexes with maltooligosaccharides as revealed by chip-nanoelectrospray high-resolution tandem mass spectrometry

Dateien

Zu diesem Dokument gibt es keine Dateien.

Datum

2015

Autor:innen

Capitan, Florina

Robu, Adrian C.

Schiopu, Catalin

Ilie, Constantin

Chait, Brian T.

Przybylski, Michael

Zamfir, Alina D.

DOI (zitierfähiger Link)

https://doi.org/10.1007/s00726-015-2030-1

Sammlungen

Chemie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Amino Acids. 2015, 47(11), pp. 2399-2407. ISSN 0939-4451. eISSN 1438-2199. Available under: doi: 10.1007/s00726-015-2030-1

Zusammenfassung

Cow's milk protein allergy in exclusively breastfed infants, the main cause of food intolerance during the first 6 months of life, is triggered by the mother's diet. β-Lactoglobulin (BLG) present in cow's milk is one of the most potent allergens for newborns. Since no prophylactic treatment is available, finding ligands capable of binding BLG and reducing its allergenicity is currently the focus of research. In this work, an innovative methodology encompassing microfluidics based on fully automated chip-nanoelectrospray ionization (nanoESI), coupled with high-resolution mass spectrometry (MS) on a quadrupole time-of-flight (QTOF MS) instrument was developed. This platform was employed for the assessment of the noncovalent interactions between maltohexaose (Glc₆) and β-lactoglobulin extracted from human milk upon deliberate intake of cow's milk. The experiments were carried out in (+) ESI mode, using ammonium acetate (pH 6.0) as the buffer and also in pure water. In both cases, the MS analysis revealed the formation of BLG-Glc₆ complex, which was characterized by top-down fragmentation in tandem MS (MS/MS) using collision-induced dissociation (CID). Our findings have a significant biomedical impact, indicating that Glc₆ binds BLG under conditions mimicking the in vivo environment and therefore might represent a ligand, able to reduce its allergenicity.

Fachgebiet (DDC)

540 Chemie

Schlagwörter

β-Lactoglobulin, Human milk, Noncovalent interaction, Maltooligosaccharides, Mass spectrometry

Zitieren

ISO 690

CAPITAN, Florina, Adrian C. ROBU, Catalin SCHIOPU, Constantin ILIE, Brian T. CHAIT, Michael PRZYBYLSKI, Alina D. ZAMFIR, 2015. β-Lactoglobulin detected in human milk forms noncovalent complexes with maltooligosaccharides as revealed by chip-nanoelectrospray high-resolution tandem mass spectrometry. In: Amino Acids. 2015, 47(11), pp. 2399-2407. ISSN 0939-4451. eISSN 1438-2199. Available under: doi: 10.1007/s00726-015-2030-1

BibTex

@article{Capitan2015Lacto-33020,
  year={2015},
  doi={10.1007/s00726-015-2030-1},
  title={β-Lactoglobulin detected in human milk forms noncovalent complexes with maltooligosaccharides as revealed by chip-nanoelectrospray high-resolution tandem mass spectrometry},
  number={11},
  volume={47},
  issn={0939-4451},
  journal={Amino Acids},
  pages={2399--2407},
  author={Capitan, Florina and Robu, Adrian C. and Schiopu, Catalin and Ilie, Constantin and Chait, Brian T. and Przybylski, Michael and Zamfir, Alina D.}
}

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Universitätsbibliographie

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