Quality Control and Ultrastructural Evaluation of Surface-modified Intraocular Lenses in vitro by Atomic Force Microscopy

Abstract Background To compare the anterior surface roughness of two commercially available posterior chamber phakic intraocular lenses (IOLs) using atomic force microscopy (AFM). Methods Four phakic IOLs were used for this prospective, experimental study: two Visian ICL EVO+ V5 lenses and two iPCL 2.0 lenses. All of them were brand new, were not previously implanted in humans, were monofocal and had a dioptric power of − 12 diopters (D). The anterior surface roughness was assessed using a JPK NanoWizard II® atomic force microscope in contact mode immersed in liquid. Olympus OMCL-RC800PSA commercial silicon nitride cantilever tips were used. Anterior surface roughness measurements were made in 7 areas of 10 × 10 μm at 512 × 512 point resolution. The roughness was measured using the root-mean-square (RMS) value within the given regions. Results The mean of all anterior surface roughness measurements was 6.09 ± 1.33 nm (nm) in the Visian ICL EVO+ V5 and 3.49 ± 0.41 nm in the iPCL 2.0 (p = 0.001). Conclusion In the current study, we found a statistically significant smoother anterior surface in the iPCL 2.0 phakic intraocular lenses compared with the VISIAN ICL EVO+ V5 lenses when studied with atomic force microscopy.

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Observation of a Polystyrene Surface Modified by Ultrasonic Scratching Using Atomic Force Microscopy

Japanese Journal of Applied Physics ◽

10.1143/jjap.38.3936 ◽

1999 ◽

Vol 38 (Part 1, No. 6B) ◽

pp. 3936-3939 ◽

Cited By ~ 1

Author(s):

Futoshi Iwata ◽

Tarou Matsumoto ◽

Ryuhei Ogawa ◽

Akira Sasaki

Keyword(s):

Atomic Force Microscopy ◽

Force Microscopy ◽

Polystyrene Surface ◽

Atomic Force ◽

Surface Modified

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Resolving the High-Resolution Architecture, Assembly and Functional Repertoire of Bacterial Systems by In Vitro Atomic Force Microscopy

Life at the Nanoscale ◽

10.1201/9780429066597-4 ◽

2019 ◽

pp. 71-98

Author(s):

Alexander J. Malkin

Keyword(s):

Atomic Force Microscopy ◽

High Resolution ◽

Force Microscopy ◽

Atomic Force ◽

Bacterial Systems

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Grain Segmentation in Atomic Force Microscopy for Thin-Film Deposition Quality Control

New Trends in Image Analysis and Processing – ICIAP 2019 - Lecture Notes in Computer Science ◽

10.1007/978-3-030-30754-7_38 ◽

2019 ◽

pp. 385-394

Author(s):

Nicolò Lanza ◽

Alessandro Romeo ◽

Marco Cristani ◽

Francesco Setti

Keyword(s):

Thin Film ◽

Atomic Force Microscopy ◽

Quality Control ◽

Thin Film Deposition ◽

Film Deposition ◽

Force Microscopy ◽

Atomic Force

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Visualization by atomic force microscopy of tobacco mosaic virus movement protein–RNA complexes formed in vitro

Journal of General Virology ◽

10.1099/0022-1317-82-6-1503 ◽

2001 ◽

Vol 82 (6) ◽

pp. 1503-1508 ◽

Cited By ~ 45

Author(s):

O. I. Kiselyova ◽

I. V. Yaminsky ◽

E. M. Karger ◽

O. Yu. Frolova ◽

Y. L. Dorokhov ◽

...

Keyword(s):

Atomic Force Microscopy ◽

Tobacco Mosaic Virus ◽

Mosaic Virus ◽

Movement Protein ◽

Structural Conversion ◽

Force Microscopy ◽

Rna Transcripts ◽

Atomic Force ◽

Rna Complexes

The structure of complexes formed in vitro by tobacco mosaic virus (TMV)-coded movement protein (MP) with TMV RNA and short (890 nt) synthetic RNA transcripts was visualized by atomic force microscopy on a mica surface. MP molecules were found to be distributed along the chain of RNA and the structure of MP–RNA complexes depended on the molar MP:RNA ratios at which the complexes were formed. A rise in the molar MP:TMV RNA ratio from 20:1 to 60–100:1 resulted in an increase in the density of the MP packaging on TMV RNA and structural conversion of complexes from RNase-sensitive ‘beads-on-a-string’ into a ‘thick string’ form that was partly resistant to RNase. The ‘thick string’-type RNase-resistant complexes were also produced by short synthetic RNA transcripts at different MP:RNA ratios. The ‘thick string’ complexes are suggested to represent clusters of MP molecules cooperatively bound to discrete regions of TMV RNA and separated by protein-free RNA segments.

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