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Leveraging nature’s biomolecular designs in next-generation protein sequencing reagent development
Next-generation approaches for protein sequencing are now emerging that could have the potential to revolutionize the field in proteomics. One such sequencing method involves fluorescence-based imaging of immobilized peptides in which the N-terminal amino acid of a polypeptide is readout sequentiall...
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Published in: | Applied microbiology and biotechnology 2020-09, Vol.104 (17), p.7261-7271 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Next-generation approaches for protein sequencing are now emerging that could have the potential to revolutionize the field in proteomics. One such sequencing method involves fluorescence-based imaging of immobilized peptides in which the N-terminal amino acid of a polypeptide is readout sequentially by a series of fluorescently labeled biomolecules. When selectively bound to a specific N-terminal amino acid, the NAAB (
N
-terminal amino acid binder) affinity reagent identifies the amino acid through its associated fluorescence tag. A key technical challenge in implementing this fluoro-sequencing approach is the need to develop NAAB affinity reagents with the high affinity and selectivity for specific N-terminal amino acids required for this biotechnology application. One approach to develop such a NAAB affinity reagent is to leverage naturally occurring biomolecules that bind amino acids and/or peptides. Here, we describe several candidate biomolecules that could be considered for this purpose and discuss the potential for developability of each.
Key points
• Next-generation sequencing methods are emerging that could revolutionize proteomics.
• Sequential readout of N-terminal amino acids by fluorescent-tagged affinity reagents.
• Native peptide/amino acid binders can be engineered into affinity reagents.
• Protein size and structure contribute to feasibility of reagent developability. |
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ISSN: | 0175-7598 1432-0614 |
DOI: | 10.1007/s00253-020-10745-2 |