Controlled movement of ssDNA conjugated peptide through <i>Mycobacterium smegmatis</i> porin A (MspA) nanopore by a helicase motor for peptide sequencing application

Chen, Zhijie; Wang, Zhenqin; Yang, Xu; Zhang, Xiaochun; Tian, Boxue; Bai, Jingwei

doi:10.1039/d1sc04342k

Cited by 43 publications

(34 citation statements)

References 39 publications

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“…This was similarly demonstrated by Chen et al. suggesting that stretching the analyte, thus limiting thermal motion would improve the resolution ( Chen et al., 2021 ). Yan et al.…”

Section: Sensing Biomedical Relevant Molecules With Biological Nanoporesmentioning

confidence: 57%

Biological nanopores for single-molecule sensing

2022

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“…This was similarly demonstrated by Chen et al. suggesting that stretching the analyte, thus limiting thermal motion would improve the resolution ( Chen et al., 2021 ). Yan et al.…”

Section: Sensing Biomedical Relevant Molecules With Biological Nanoporesmentioning

confidence: 57%

Biological nanopores for single-molecule sensing

2022

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“…8 The other strategy employs DNA motor enzymes to ratchet a peptide–oligonucleotide conjugate into the nanopore. 6,7,9 The former method requires the digestion of the protein. Then, all peptide fragments should be captured and recognized by a nanopore.…”

Section: Introductionmentioning

confidence: 99%

An engineered third electrostatic constriction of aerolysin to manipulate heterogeneously charged peptide transport

2022

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“…One of the major concerns of OmpF sensing peptides is the short residence time; many approaches can potentially be utilized to boost the peptide sensing capability through nanopores, e.g. forming peptide-DNA conjugation for enzymedirected amino acid stepwise scanning (10,24,25). Moreover, we found strong indications that the chirality of the polar sidechain from serine (Mol-13) creates additional interactions with the residues in the CZ of OmpF (e.g.…”

mentioning

confidence: 80%

Identification of single amino acid chiral and positional isomers using an electrostatically asymmetric nanopore

Wang

Prajapati

Gao

et al. 2022

Preprint

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Chirality is essential in nearly all biological organization and chemical reaction but is rarely considered due to technical limitations in identifying L/D isomerization. Using OmpF, a membrane channel from E. coli with an electrostatically asymmetric constriction zone, allows discriminating chiral amino acids in a single peptide. The heterogeneous distribution of charged residues in OmpF causes a strong asymmetric electrostatic field at the constriction. This asymmetry forces the sidechains of the peptides to specific orientations within OmpF, causing distinct ion current fluctuations. Using a statistical analysis of the respective ion current variations allows distinguishing the presence and position of each chiral amino acid. To explore potential applications, the disease-related peptide β-Amyloid, and its D-Asp1 isoform, as well as a mixture of the Icatibant peptide drug (HOE 140) and its D-Ser7 mutant, have been discriminated. Both chiral isomers were not applicable to be distinguished by mass spectrum approaches. These findings highlight a novel sensing mechanism for identifying single amino acids in single peptides and even for achieving single-molecule protein sequencing.

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Controlled movement of ssDNA conjugated peptide through Mycobacterium smegmatis porin A (MspA) nanopore by a helicase motor for peptide sequencing application

Abstract: A new technique for single molecular peptide sequencing is demonstrated by translocation of ssDNA-conjugated-peptide through MspA nanopore which is regulated by a DNA helicase motor.

Cited by 43 publications

References 39 publications

Biological nanopores for single-molecule sensing

Biological nanopores for single-molecule sensing

An engineered third electrostatic constriction of aerolysin to manipulate heterogeneously charged peptide transport

Identification of single amino acid chiral and positional isomers using an electrostatically asymmetric nanopore

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