In-solution buffer-free digestion allows full-sequence coverage and complete characterization of post-translational modifications of the receptor-binding domain of SARS-CoV-2 in a single ESI-MS spectrum.
Amino Acid Sequence
Cysteine
/ chemistry
Humans
Hydrophobic and Hydrophilic Interactions
Peptide Fragments
/ chemistry
Protein Binding
Protein Domains
Protein Processing, Post-Translational
Protein Subunits
Spectrometry, Mass, Electrospray Ionization
/ methods
Spike Glycoprotein, Coronavirus
/ chemistry
Buffer-free digestion
Hydrophilic peptides
Modified cysteine
RBD
SARS-CoV-2
Journal
Analytical and bioanalytical chemistry
ISSN: 1618-2650
Titre abrégé: Anal Bioanal Chem
Pays: Germany
ID NLM: 101134327
Informations de publication
Date de publication:
Dec 2021
Dec 2021
Historique:
received:
15
06
2021
accepted:
05
10
2021
revised:
16
09
2021
pubmed:
6
11
2021
medline:
15
12
2021
entrez:
5
11
2021
Statut:
ppublish
Résumé
Subunit vaccines based on the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 provide one of the most promising strategies to fight the COVID-19 pandemic. The detailed characterization of the protein primary structure by mass spectrometry (MS) is mandatory, as described in ICHQ6B guidelines. In this work, several recombinant RBD proteins produced in five expression systems were characterized using a non-conventional protocol known as in-solution buffer-free digestion (BFD). In a single ESI-MS spectrum, BFD allowed very high sequence coverage (≥ 99%) and the detection of highly hydrophilic regions, including very short and hydrophilic peptides (2-8 amino acids), and the His
Identifiants
pubmed: 34739558
doi: 10.1007/s00216-021-03721-w
pii: 10.1007/s00216-021-03721-w
pmc: PMC8569510
doi:
Substances chimiques
Peptide Fragments
0
Protein Subunits
0
Spike Glycoprotein, Coronavirus
0
spike protein, SARS-CoV-2
0
Cysteine
K848JZ4886
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
7559-7585Subventions
Organisme : CIGB
ID : This research was supported by the Grant awarded t
Informations de copyright
© 2021. Springer-Verlag GmbH Germany, part of Springer Nature.
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