Amino Acid Translocation Through a Dual Nanopore Platform
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arXiv
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| Main Authors: | , , , , , , , |
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| Format: | Preprint |
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2025
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| _version_ | 1866915692972867584 |
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| author | Lin, Chih-Yuan Bhatia, Pia Uy-Tioco, Alexandra Sofia Kavetsky, Kyril Morral, Celia Keneipp, Rachael Pradeep, Namrata Drndic, Marija |
| author_facet | Lin, Chih-Yuan Bhatia, Pia Uy-Tioco, Alexandra Sofia Kavetsky, Kyril Morral, Celia Keneipp, Rachael Pradeep, Namrata Drndic, Marija |
| contents | We demonstrate a dual nanopore platform (DNP) containing a top 2D MoS2 pore in series with a 3 to 5 nm thick SiN pore, vertically separated by 30 nm, with diameters of 1.0 and 3.0 nm, respectively. This platform enables independent probing of analytes by each pore, thereby providing complementary information. We measure translocations of single amino acids (AA) and evaluate current blockades recorded across the two pores upon applying voltage. Small diameters ensured tight passage of individual AAs through the nanopores and provided a good signal-tonoise ratio (RMS current noise of 16 pA_RMS and SNR = 6). We focus on measurements of O-Phospho-L-tyrosine at 400 mV, demonstrating single amino acid detection and a good quantitative agreement with the calculated open pore and blocked currents. Based on these results, future device performance can benefit from slightly smaller pores, specifically the SiN pore, higher voltages and electrolyte concentration, and lower system noise. |
| format | Preprint |
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arxiv_https___arxiv_org_abs_2512_20776 |
| institution | arXiv |
| publishDate | 2025 |
| record_format | arxiv |
| spellingShingle | Amino Acid Translocation Through a Dual Nanopore Platform Lin, Chih-Yuan Bhatia, Pia Uy-Tioco, Alexandra Sofia Kavetsky, Kyril Morral, Celia Keneipp, Rachael Pradeep, Namrata Drndic, Marija Applied Physics Other Condensed Matter We demonstrate a dual nanopore platform (DNP) containing a top 2D MoS2 pore in series with a 3 to 5 nm thick SiN pore, vertically separated by 30 nm, with diameters of 1.0 and 3.0 nm, respectively. This platform enables independent probing of analytes by each pore, thereby providing complementary information. We measure translocations of single amino acids (AA) and evaluate current blockades recorded across the two pores upon applying voltage. Small diameters ensured tight passage of individual AAs through the nanopores and provided a good signal-tonoise ratio (RMS current noise of 16 pA_RMS and SNR = 6). We focus on measurements of O-Phospho-L-tyrosine at 400 mV, demonstrating single amino acid detection and a good quantitative agreement with the calculated open pore and blocked currents. Based on these results, future device performance can benefit from slightly smaller pores, specifically the SiN pore, higher voltages and electrolyte concentration, and lower system noise. |
| title | Amino Acid Translocation Through a Dual Nanopore Platform |
| topic | Applied Physics Other Condensed Matter |
| url | https://arxiv.org/abs/2512.20776 |