Chemical treatment of mica for atomic force microscopy can affect biological sample conformation

Costa, Lucas Teixeira; Pinto, José R.; Moraes, Marta Bueno de; Souza, Guttierre G.B. de; Sorenson, Martha M.; Bisch, Paulo Mascarello; Weissmüller, Gilberto

doi:10.1016/j.bpc.2003.10.011

Cited by 10 publications

(6 citation statements)

References 26 publications

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“…A bare mica surface adsorbs DNA and various proteins by electrostatic interaction. We can control the adsorption strength by varying the ionic strength or pH or by adding divalent cations such as Mg 2+ and Ni 2+ (especially for attaching negatively charged samples) (17,72). Monovalent cations markedly change the affinity; Li + > Na + > K + for every protein (18).…”

Section: Substrate Surfacesmentioning

confidence: 99%

High-Speed AFM and Applications to Biomolecular Systems

Ando

Uchihashi

Kodera

2013

Annu. Rev. Biophys.

250

216

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Directly observing individual protein molecules in action at high spatiotemporal resolution has long been a holy grail for biological science. This is because we long have had to infer how proteins function from the static snapshots of their structures and dynamic behavior of optical makers attached to the molecules. This limitation has recently been removed to a large extent by the materialization of high-speed atomic force microscopy (HS-AFM). HS-AFM allows us to directly visualize the structure dynamics and dynamic processes of biological molecules in physiological solutions, at subsecond to sub-100-ms temporal resolution, without disturbing their function. In fact, dynamically acting molecules such as myosin V walking on an actin filament and bacteriorhodopsin in response to light are successfully visualized. In this review, we first describe theoretical considerations for the highest possible imaging rate of this new microscope, and then highlight recent imaging studies. Finally, the current limitation and future challenges to explore are described.

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Section: Substrate Surfacesmentioning

confidence: 99%

High-Speed AFM and Applications to Biomolecular Systems

Ando

Uchihashi

Kodera

2013

Annu. Rev. Biophys.

250

216

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“…Divalent cation dependent binding may also be mediated by the charge on protein residues alone. Negatively charged chicken skeletal muscle F-actin (theoretical pI 5.26, Swiss-Prot P20111) bound to Ni 2+ -treated but not to untreated mica (Costa et al, 2004). Both fibrillin and type VI collagen are negatively charged.…”

Section: Introductionmentioning

confidence: 97%

“…Although the mechanism that pulls DNA molecules onto the surface in the presence of divalent counterions is still not fully understood (Pastre et al, 2003), both surface-multivalent cation-DNA charge bridges (Hansma and Laney, 1996;Bezanilla et al, 1995), and correlations in surface and DNA multivalent cation charge clouds (Pastre et al, 2003;Ellis et al, 2004) have been proposed. Divalent cation (Ni 2+ ) dependent binding to mica has also been demonstrated for proteins of the mucin family and for skeletal muscle F-actin (Costa et al, 2004;McMaster et al, 1999;Brayshaw et al, 2003). Mucins are glycoproteins and their charge characteristics are dominated by sialic acid and sulphate moieties on the oligosaccharide side chains which may comprise up to 80% of the dry weight (Ellingham et al, 1999;Lamblin et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

“…The concentration and valency of charged solutes has been shown to play a key role in the adsorption of negatively Matrix Biology 26 (2007) 156 -166 www.elsevier.com/locate/matbio charged biomolecules to negatively charged surfaces (Hansma and Laney, 1996). Freshly cleaved mica, which provides an atomically flat surface for the deposition of biological molecules, has been used extensively as a substrate in atomic force microscopy (AFM) and electron microscopy studies (Thundat et al, 1992;Costa et al, 2004;Mould et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

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The morphology of adsorbed extracellular matrix assemblies is critically dependent on solution calcium concentration

et al. 2007

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“…The substrate of choice for AFM imaging is dependent upon the biopolymer to be studied. Ultra-flat muscovite or ruby mica are commonly employed for DNA, proteins and RNA [37,38]. Other common substrates include gold, silicon and glass [39].…”

Section: Afm Instrumentationmentioning

confidence: 99%

Molecular-Scale Studies on Biopolymers Using Atomic Force Microscopy

Ellis

Allen

Chim

et al.

Polymer Therapeutics II

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The atomic force microscope (AFM) is capable of acquiring a range of structural and physicochemical information on a wide range of biopolymers. The ability to achieve nanoscale resolution, coupled with the potential to image and manipulate realtime molecular-scale events, suggests that AFM is one of the most promising techniques available for the study of biopolymers. AFM offers the potential to obtain a wide range of both quantitative and qualitative information on biopolymers, ranging from their conformations in physiological buffers to the forces involved in bond cleavage. This review explores the most common modes of AFM operation including imaging (contact and tapping mode) and force spectroscopy. The application of these modes to biopolymer characterisation will be discussed, with an emphasis on key studies.

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Chemical treatment of mica for atomic force microscopy can affect biological sample conformation

Cited by 10 publications

References 26 publications

High-Speed AFM and Applications to Biomolecular Systems

High-Speed AFM and Applications to Biomolecular Systems

The morphology of adsorbed extracellular matrix assemblies is critically dependent on solution calcium concentration

Molecular-Scale Studies on Biopolymers Using Atomic Force Microscopy

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