Submitted:
31 December 2025
Posted:
01 January 2026
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Abstract
L-asparaginase (L-Aspase) enzyme has found applications in medicine for treatment of various cancers. Herein, we report single-molecule study of thermal denaturation of L-Aspase within 25°C to 60°C temperature range by atomic force microscopy (AFM) and by single-molecule sensing with a (solid state nanopore)-based electrical detector (SSNPED). AFM has allowed us to reveal a thermally induced changes in aggregation state of L-Aspase and in its adsorbability on mica. At the same time, the configuration of the enzyme’s globule spatial conformation has been found to alter according to data obtained with the SSNPED. Our results reported open up opportunities for further development of anti-cancer drugs.
Keywords:
L-asparaginase
; solid-state nanopore
; thermal denaturation
; atomic force microscopy
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