Evaluation of Medicine Effects on the Interaction
of Myoglobin and Its Aptamer or Antibody Using Atomic Force Microscopy
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Abstract
The effects of medicine on the biomolecular
interaction have been
given increasing attention in biochemistry and affinity-based analytics
since the environment in vivo is complex especially for the patients.
Herein, myoglobin, a biomarker of acute myocardial infarction, was
used as a model, and the medicine effects on the interactions of myoglobin/aptamer
and myoglobin/antibody were systematically investigated using atomic
force microscopy (AFM) for the first time. The results showed that
the average binding force and the binding probability of myoglobin/aptamer
almost remained unchanged after myoglobin-modified gold substrate
was incubated with promazine, amoxicillin, aspirin, and sodium penicillin,
respectively. These parameters were changed for myoglobin/antibody
after the myoglobin-modified gold substrate was treated with these
medicines. For promazine and amoxicillin, they resulted in the change
of binding force distribution of myoglobin/antibody (i.e., from unimodal
distribution to bimodal distribution) and the increase of binding
probability; for aspirin, it only resulted in the change of the binding
force distribution, and for sodium penicillin, it resulted in the
increase of the average binding force and the binding probability.
These results may be attributed to the different interaction modes
and binding sites between myoglobin/aptamer and myoglobin/antibody,
the different structures between aptamer and antibody, and the effects
of medicines on the conformations of myoglobin. These findings could
enrich our understanding of medicine effects on the interactions of
aptamer and antibody to their target proteins. Moreover, this work
will lay a good foundation for better research and extensive applications
of biomolecular interaction, especially in the design of biosensors
in complex systems