Identification by FT-ICR-MS of Camelus dromedarius α-lactalbumin variants as the result of nonenzymatic deamidation of Asn-16 and Asn-45

Abstract : Nonenzymatic deamidation of asparaginyl residues can occur spontaneously under physiological conditions principally when a glycyl residue is at the carboxyl side of Asn and leads to formation of aspartyl and isoaspartyl residues. This modification can change the biological activity of proteins or peptides and trigger an auto-immune response. The α-lactalbumins of members of the Camelidae family are the only of described α-lactalbumins that carry two AsnGly sequences. In the present study, high-resolution mass spectrometry, which enables accurate mass measurement has shown that Asn16 and Asn45 underwent a nonenzymatic deamidation, the sequence Asn45–Gly46 being deamidated spontaneously at near-neutral and basic pH and Asn16–Gly17 rather at basic pH. The 16–17 sequence was probably stabilized at near-neutral pH by hydrogen bonds according to the molecular modelisation performed with the camel protein.
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Food Chemistry, Elsevier, 2015, 187, pp.305 - 313. 〈10.1016/j.foodchem.2015.04.036〉
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https://hal.univ-lorraine.fr/hal-01522025
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Soumis le : vendredi 12 mai 2017 - 16:31:53
Dernière modification le : lundi 19 mars 2018 - 15:08:42

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Saliha Si Ahmed Zennia, Abderrahmane Mati, Franck Saulnier, Yann Verdier, Giovanni Chiappetta, et al.. Identification by FT-ICR-MS of Camelus dromedarius α-lactalbumin variants as the result of nonenzymatic deamidation of Asn-16 and Asn-45. Food Chemistry, Elsevier, 2015, 187, pp.305 - 313. 〈10.1016/j.foodchem.2015.04.036〉. 〈hal-01522025〉

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