On possible trypsin-induced biases in peptides analysis with aerolysin nanopore.
aerolysin
enzymatic degradation
low-abundance
nanopore
peptides
Journal
Proteomics
ISSN: 1615-9861
Titre abrégé: Proteomics
Pays: Germany
ID NLM: 101092707
Informations de publication
Date de publication:
06 2022
06 2022
Historique:
revised:
17
03
2022
received:
01
06
2021
accepted:
23
03
2022
pubmed:
1
4
2022
medline:
14
6
2022
entrez:
31
3
2022
Statut:
ppublish
Résumé
Nanopore-based single-molecule analysis technique is a promising approach in the field of proteomics. In this Technical Brief, the interaction between the biological nanopore of Aerolysin (AeL) and peptides is investigated, focusing on potential biases depending on the AeL activation protocol. Our results reveal that residual trypsin, which may be unintentionally introduced in analyte solution when using a classical AeL activation protocol, can induce a significant formation of shorter peptides by enzymatic degradation of longer ones, which may lead to unwanted effects and/or misinterpretations. AeL free-trypsin activation protocol eliminates this bias and appears more appropriate for peptide/proteins analysis, specifically in the perspective of nanopore-based molecular fingerprinting or of low-abundance species characterization.
Identifiants
pubmed: 35357771
doi: 10.1002/pmic.202100056
doi:
Substances chimiques
Bacterial Toxins
0
Peptides
0
Pore Forming Cytotoxic Proteins
0
aerolysin
53126-24-2
Trypsin
EC 3.4.21.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2100056Informations de copyright
© 2022 Wiley-VCH GmbH.
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