CH-π Interactions Elucidated at the Single-Molecule Level.

CH-π interactions represent a weak yet significant molecular force that is prevalent in diverse biological and chemical systems. Despite compelling evidence supporting the existence of CH-π interactions, experimentally measuring these weak interactions remains challenging due to the coexistence of numerous stronger noncovalent interactions. Here, we construct a refined system to accurately compare the strength of CH-π interactions between phenylalanine derivatives and aliphatic amino acids through molecular exchange processes inside a protein nanopore.

Nanopore-based enzyme-linked immunosorbent assay for cancer biomarker detection.

Enzyme-linked immunosorbent assay (ELISA) has been widely used in cancer diagnostics due to its specificity, sensitivity and high throughput. However, conventional ELISA is semiquantitative and has an insufficiently low detection limit for applications requiring ultrahigh sensitivity. In this study, we developed an α-hemolysin-nanopore-based ELISA for detecting cancer biomarkers.

Nanopore-Based High-Resolution Detection of Multiple Post-Translational Modifications in Protein.

Protein post-translational modifications (PTMs) play crucial roles in various cellular processes. Despite their significance, only a few PTMs have been extensively studied at the proteome level, primarily due to the scarcity of reliable, convenient, and low-cost sensing methods. Here, we present a straightforward and effective strategy for detecting PTMs on short peptides through host-guest interaction-assisted nanopore sensing.

Single-Molecule Exchange inside a Nanocage Provides Insights into the Origin of π-π Interactions.

The attractive interactions between aromatic rings, also known as π-π interactions, have been widely used for decades. However, the origin of π-π interactions remains controversial due to the difficulties in experimentally measuring the weak interactions between π-systems. Here, we construct an elaborate system to accurately compare the strength of the π-π interactions between phenylalanine derivatives via molecular exchange processes inside a protein nanopore.