Non-Linear Dynamics of Microcantilevers in Liquid Environment Atomic Force Microscopy When Operating at the Second Eigenmode: Subharmonics, Multiple Impacts, and Chaos

Author(s):  
Daniel R. Kiracofe ◽  
Arvind Raman

Many newer atomic force microscopy (AFM) methods aim to excite higher-order eigenmodes of the microcantilevers in multi-frequency excitation/detection schemes for improving compositional contrast in nanoscale imaging. Yet, before moving to multi-mode excitation schemes it is important to understand how, if at all, operating the microscope at eigenmodes beyond the fundamental is different from operating at the fundamental eigenmode. This question becomes particularly relevant for biological applications when cantilevers are operated in liquid environments, which is critical for studying biological processes under physiological “native” conditions. In this work, the dynamics of AFM cantilevers in liquids are investigated when the cantilever is driven at its second natural frequency — a situation, which from prior work in air or vacuum, ought not be essentially different from operating at the first natural frequency. The dynamics of cantilevers in liquids tapping on samples are in fact found to be surprisingly different when operating at the second eigenmode. A complex set of behaviors are found including sub-harmonic (e.g. only one impact every four drive cycles), drum-roll like multiple-impacts (e.g.two or three impacts every drive cycle) and chaotic. The subharmonic behaviors, in particular, have not been studied before in liquids and are not accounted for in any current method. These behaviors are demonstrated through numerical simulations and confirmed with experiments.

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Lukas Stühn ◽  
Julia Auernhammer ◽  
Christian Dietz

AbstractFerritin, a protein that is present in the human body for a controlled iron storage and release, consists of a ferrihydrite core and a protein shell. Apoferritin, the empty shell of ferritin, can be modified to carry tailored properties exploitable for targeted and direct drug delivery. This protein shell has the ability to dis- and reassemble depending on the pH value of the liquid environment and can thus be filled with the desired substance. Here we observed the dis- and reassembly process of the protein shell of ferritin and apoferritin in situ and in real space using atomic force microscopy. Ferritin and apoferritin nanoparticles adsorbed on a mica substrate exhibited a change in their size by varying the pH value of the surrounding medium. Lowering the pH value of the solution led to a decrease in size of the nanoparticles whereas a successive increase of the pH value increased the particle size again. The pH dependent change in size could be related to the dis- and reassembling of the protein shell of ferritin and apoferritin. Supplementary imaging by bimodal magnetic force microscopy of ferritin molecules accomplished in air revealed a polygonal shape of the core and a three-fold symmetry of the protein shell providing valuable information about the substructure of the nanoparticles.


RSC Advances ◽  
2019 ◽  
Vol 9 (47) ◽  
pp. 27464-27474 ◽  
Author(s):  
Xinfeng Tan ◽  
Dan Guo ◽  
Jianbin Luo

Dynamic force microscopy (DFM) has become a multifunctional and powerful technique for the study of the micro–nanoscale imaging and force detection, especially in the compositional and nanomechanical properties of polymers.


2009 ◽  
Vol 1 (2) ◽  
pp. 168-180 ◽  
Author(s):  
David Alsteens ◽  
Etienne Dague ◽  
Claire Verbelen ◽  
Guillaume Andre ◽  
Vincent Dupres ◽  
...  

2008 ◽  
Vol 32 ◽  
pp. 49-52 ◽  
Author(s):  
Chun Chih Lai ◽  
John M. Bell ◽  
Nunzio Motta

A new, direct method has been developed to measure the adhesion forces of bovine serum albumin (BSA) on surfaces by using Atomic Force Microscopy (AFM) in liquid environment. We were able to measure interactions between proteins and substrate surface in PBS solution directly without any modification to the substrate or the AFM tip. Two different surfaces have been used in the experiments: mica (hydrophilic surface) and polystyrene (hydrophobic surface). The results show that a polystyrene surface is more adhesive to BSA than a mica surface. This is consistent with previous research, which assessed that hydrophobic surfaces enhance protein adhesion but hydrophilic surfaces do not, demonstrating the effectiveness of the technique.


2001 ◽  
Vol 72 (S1) ◽  
pp. S129-S132 ◽  
Author(s):  
S.P. Jarvis ◽  
T. Ishida ◽  
T. Uchihashi ◽  
Y. Nakayama ◽  
H. Tokumoto

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