Abstract

We estimate the elasticity of single polymer chains using atomic force microscope (AFM)-based oscillatory experiments. An accurate estimate of elasticity using AFM is limited by assumptions in describing the dynamics of an oscillating cantilever. Here, we use a home-built fiber-interferometry-based detection system that allows a simple and universal point-mass description of cantilever oscillations. By oscillating the cantilever base and detecting changes in cantilever oscillations with an interferometer, we extracted stiffness versus extension profiles for polymers. For polyethylene glycol (PEG) in a good solvent, stiffness–extension data showed significant deviation from conventional force–extension curves (FECs) measured in constant velocity pulling experiments. Furthermore, modeling stiffness data with an entropic worm-like chain (WLC) model yielded a persistence length of (0.5 ± 0.2 nm) compared to anomaly low value (0.12 nm ± 0.01) in conventional pulling experiments. This value also matched well with equilibrium measurements performed using magnetic tweezers. In contrast, polystyrene (PS) in a poor solvent, like water, showed no deviation between the two experiments. However, the stiffness profile for PS in good solvent (8M Urea) showed significant deviation from conventional force–extension curves. We obtained a persistence length of (0.8 ± 0.2 nm) compared to (0.22 nm ± 0.01) in pulling experiments. Our unambiguous measurements using interferometer yield physically acceptable values of persistence length. It validates the WLC model in good solvents but suggests caution for its use in poor solvents.

Highlights

  • Single-molecule force spectroscopy (SMFS) experiments are indispensable in studying biomolecules and other polymeric complexes at the single-molecule level [1]

  • Single-molecule force–extension curves are sensitive to artifacts and can be misinterpreted as a valid single-molecule trajectory

  • As a polymer is pulled with atomic force microscope (AFM), force-extension curves (FECs) report the entropic nature of polymer elasticity due to vast changes in conformational space

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Summary

Introduction

Received: 26 November 2021Single-molecule force spectroscopy (SMFS) experiments are indispensable in studying biomolecules and other polymeric complexes at the single-molecule level [1]. A number of experiments [5,6,7,8,9] and simulations [10,11] have considered separating intrinsic thermodynamic and kinetic signatures of molecule from effects of instrument. These studies consider effects like finite response time of AFM cantilever probe and/or its stiffness on the accuracy of extracting parameters of a molecule’s landscape

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