Back and forth with nanopore peptide sequencing

Article Chemistry, Multidisciplinary

Bottom-up fabrication of a proteasome-nanopore that unravels and processes single proteins

Shengli Zhang et al.

Summary: This research utilized components from all three domains of life to construct a multiprotein complex that controls the unfolding and threading of individual proteins across a nanopore. By designing a stable and low-noise beta-barrel nanopore sensor and integrating a proteasome, the study achieved the unfolding and linearized transport of proteins, opening up new approaches for single-molecule protein analysis.

NATURE CHEMISTRY (2021)

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Article Multidisciplinary Sciences

Multiple rereads of single proteins at single-amino acid resolution using nanopores

Henry Brinkerhoff et al.

Summary: This study presents a nanopore-based single-molecule peptide reader capable of identifying single amino acid substitutions within individual peptides with high accuracy. By pulling a DNA-peptide conjugate through a biological nanopore and reading the ion current signal, discrimination of single amino acid substitutions in single reads was achieved. The ability to obtain numerous independent reads of the same molecule and achieve a low error rate in amino acid variant identification signifies a promising advancement towards single-molecule protein fingerprinting and analysis technology.

SCIENCE (2021)

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Article Multidisciplinary Sciences

Protein identification by nanopore peptide profiling

Florian Leonardus Rudolfus Lucas et al.

Summary: Nanopores can be used for protein identification by measuring peptide spectra produced from hydrolyzed proteins. The spectra from nanopore experiments and mass spectrometry share similar profiles, enabling protein fingerprinting. This approach is quantitative, showing the potential of a low-cost, portable nanopore-based analyzer for protein identification.

NATURE COMMUNICATIONS (2021)

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Article Chemistry, Multidisciplinary

Single Molecule Ratcheting Motion of Peptides in a Mycobacterium smegmatis Porin A (MspA) Nanopore

Shuanghong Yan et al.

Summary: Proteins exhibit diverse functions due to their variable amino acid sequences, but current technology for direct protein sequence analysis remains inadequate. The development of nanopore sequencing has sparked efforts to sequence peptides in a similar manner, successfully achieving direct observation of peptide's ratcheting motion and showing potential for peptide fingerprinting.

NANO LETTERS (2021)

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Article Chemistry, Multidisciplinary

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

Zhijie Chen et al.

Summary: The study presents a strategy to control peptide translocation through the MspA nanopore, achieving a read length of up to 17 amino acids and demonstrating the feasibility of distinguishing between different amino acid residues or phosphorylation sites. Further engineering of MspA-M2 may be required to improve resolution.

CHEMICAL SCIENCE (2021)

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Article Biotechnology & Applied Microbiology