4.8 Article

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

期刊

NANO LETTERS
卷 21, 期 15, 页码 6703-6710

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acs.nanolett.1c02371

关键词

MspA; nanopore; sequencing; POC; single molecule; peptide; protein

资金

  1. National Natural Science Foundation of China [31972917, 91753108, 21675083]
  2. Fundamental Research Funds for the Central Universities [020514380257, 020514380261]
  3. Programs for high-level entrepreneurial and innovative talents introduction of Jiangsu Province (Individual and Group programs)
  4. Natural Science Foundation of Jiangsu Province [BK20200009]
  5. Excellent Research Program of Nanjing University [ZYJH004]
  6. Shanghai Municipal Science and Technology Major Project, State Key Laboratory of Analytical Chemistry for Life Science [5431ZZXM1902]
  7. Technology innovation fund program of Nanjing University

向作者/读者索取更多资源

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.
Diverse functions of proteins, including synthesis, catalysis, and signaling, result from their highly variable amino acid sequences. The technology allowing for direct analysis of protein sequences, however, is still unsatisfactory. Recent developments of nanopore sequencing of DNA or RNA have motivated attempts to realize nanopore sequencing of peptides in a similar manner. The core challenge has been to achieve a controlled ratcheting motion of the target peptide, which is currently restricted to a limited choice of compatible enzymes. By constructing peptide-oligonucleotide conjugates (POCs) and measurements with nanopore-induced phase-shift sequencing (NIPSS), direct observation of the ratcheting motion of peptides has been successfully achieved. The generated events show a clear sequence dependence on the peptide that is being tested. The method is compatible with peptides with either a conjugated N- or C-terminus. The demonstrated results suggest a proof of concept of nanopore sequencing of peptide and can be useful for peptide fingerprinting.

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