Atomic Force Microscopy-Based Force Spectroscopy …
597
stretching have been defined in another study by the Dufrene team [32]. Similarly,
Muller group characterized G-protein coupled receptors by AFM-SMFS [36]. The
application of in situ AFM and FS to investigate the structure and function of cell
membranes has recently been shown by the Wang group [34].
6.1 AFM-SMFS for Determining Interactions Between
Biomolecules and MI
Biomolecules such as DNA, polysaccharides, peptides, and proteins serve an essential role in control, metabolism, communication, development, sensing, and reproduction in larger species. In order to research these extremely significant interactions
between biomolecules and MI, further studies have been carried out using various
methods. In all these techniques, SMFS is a straightforward and powerful method
for quantifying these interactions precisely. Most of the interactions of biomolecules
(DNA, proteins, polysaccharides, peptides, antigens, and antibodies) with MI have
been discussed here.
6.1.1 Probing Protein–MI Interactions
AFM-SMFS is a quite effective technique for investigating folding and unfolding
of the protein [38–40] as well as for investigating molecular interactions between
protein-functionalized tip and special MI. It is well known that aggregation and
misfolding of the proteins are associated with certain diseases like cancers, so AFMSMFS can also be used in the biomedical field [38, 40].
6.1.2 Probing Protein–inorganic MI Interactions
The most widely utilized substrates for the AFM-SMFS studies include gold and
mica. Several researchers have used AFM-SMFS to study protein and inorganic MI
molecular interactions. For example, Botello et al. have investigated the mechanical unfolding of the human cardiac titin I27 domain under thermal and chemical
denaturing conditions [39].
6.2 Determining Peptide–MI Interactions
Peptides are made of monomers of amino acids to form short chains connected
together by bonds of peptides (amides) that may directly bind to many materials,
including, for example, protein polymers and inorganic materials. Evaluating the
597
stretching have been defined in another study by the Dufrene team [32]. Similarly,
Muller group characterized G-protein coupled receptors by AFM-SMFS [36]. The
application of in situ AFM and FS to investigate the structure and function of cell
membranes has recently been shown by the Wang group [34].
6.1 AFM-SMFS for Determining Interactions Between
Biomolecules and MI
Biomolecules such as DNA, polysaccharides, peptides, and proteins serve an essential role in control, metabolism, communication, development, sensing, and reproduction in larger species. In order to research these extremely significant interactions
between biomolecules and MI, further studies have been carried out using various
methods. In all these techniques, SMFS is a straightforward and powerful method
for quantifying these interactions precisely. Most of the interactions of biomolecules
(DNA, proteins, polysaccharides, peptides, antigens, and antibodies) with MI have
been discussed here.
6.1.1 Probing Protein–MI Interactions
AFM-SMFS is a quite effective technique for investigating folding and unfolding
of the protein [38–40] as well as for investigating molecular interactions between
protein-functionalized tip and special MI. It is well known that aggregation and
misfolding of the proteins are associated with certain diseases like cancers, so AFMSMFS can also be used in the biomedical field [38, 40].
6.1.2 Probing Protein–inorganic MI Interactions
The most widely utilized substrates for the AFM-SMFS studies include gold and
mica. Several researchers have used AFM-SMFS to study protein and inorganic MI
molecular interactions. For example, Botello et al. have investigated the mechanical unfolding of the human cardiac titin I27 domain under thermal and chemical
denaturing conditions [39].
6.2 Determining Peptide–MI Interactions
Peptides are made of monomers of amino acids to form short chains connected
together by bonds of peptides (amides) that may directly bind to many materials,
including, for example, protein polymers and inorganic materials. Evaluating the