2023
DOI: 10.1016/j.actbio.2023.07.028
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In situ mapping of biomineral skeletal proteins by molecular recognition imaging with antibody-functionalized AFM tips

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Cited by 2 publications
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“…Although this fascinating scientific area is not covered in this article, we refer the reader to valuable reviews that delve into various aspects of this topic. 22–25 We also note recent reports describing the use of vibrational spectroscopy 26 and scanning probe methods 27 in relation to biomineralization. Similarly, this review does not encompass the synthesis of calcium carbonate particles with controlled morphology and size, as an excellent review article on this subject has recently been published.…”
Section: Introductionmentioning
confidence: 81%
“…Although this fascinating scientific area is not covered in this article, we refer the reader to valuable reviews that delve into various aspects of this topic. 22–25 We also note recent reports describing the use of vibrational spectroscopy 26 and scanning probe methods 27 in relation to biomineralization. Similarly, this review does not encompass the synthesis of calcium carbonate particles with controlled morphology and size, as an excellent review article on this subject has recently been published.…”
Section: Introductionmentioning
confidence: 81%
“…Herein, MET dimers and the effect of their inhibitors were analyzed from the perspective of stability by atomic force microscopy (AFM) force spectroscopy. AFM can detect the stability, tensile strength, and dissociation kinetics of single molecular bonds with piconewton sensitivity. What is more, the information provided by AFM force spectroscopy techniques does not require averaging of inhomogeneities, which is very different from block experiments in molecular assemblies. This provides the potential to assess subtle differences in the stability of the MET dimers. As shown in Scheme A, the MET protein was modified at the tip and substrate, respectively, and in order to maintain the viability and correct conformation of the MET protein, the MET protein was separated from the tip and substrate using a flexible PEG linker and protein A, respectively.…”
mentioning
confidence: 99%