Imaging Mass Spectrometry by Matrix-Assisted Laser DesorptionIonization and Stress-Strain Measurements in Iontophoresis Transepithelial Corneal Collagen Cross-Linking

Joint Authors

Azzolini, Claudio
Vinciguerra, Riccardo
Vinciguerra, Paolo
Mencucci, Rita
Spoerl, Eberhard
Camesasca, Fabrizio I.
Favuzza, Eleonora
Mastropasqua, Rodolfo
Romano, Vito

Source

BioMed Research International

Issue

Vol. 2014, Issue 2014 (31 Dec. 2014), pp.1-12, 12 p.

Publisher

Hindawi Publishing Corporation

Publication Date

2014-09-02

Country of Publication

Egypt

No. of Pages

12

Main Subjects

Medicine

Abstract EN

Purpose.

To compare biomechanical effect, riboflavin penetration and distribution in transepithelial corneal collagen cross-linking with iontophoresis (I-CXL), with standard cross linking (S-CXL) and current transepithelial protocol (TE-CXL).

Materials and Methods.

The study was divided into two different sections, considering, respectively, rabbit and human cadaver corneas.

In both sections corneas were divided according to imbibition protocols and irradiation power.

Imaging mass spectrometry by matrix-assisted laser desorption/ionization (MALDI-IMS) and stress-strain measurements were used.

Forty-eight rabbit and twelve human cadaver corneas were evaluated.

Results.

MALDI-IMS showed a deep riboflavin penetration throughout the corneal layers with I-CXL, with a roughly lower concentration in the deepest layers when compared to S-CXL, whereas with TE-CXL penetration was considerably less.

In rabbits, there was a significant increase (by 71.9% and P=0.05) in corneal rigidity after I-CXL, when compared to controls.

In humans, corneal rigidity increase was not significantly different among the subgroups.

Conclusions.

In rabbits, I-CXL induced a significant increase in corneal stiffness as well as better riboflavin penetration when compared to controls and TE-CXL but not to S-CXL.

Stress-strain in human corneas did not show significant differences among techniques, possibly because of the small sample size of groups.

In conclusion, I-CXL could be a valid alternative to S-CXL for riboflavin delivery in CXL, preserving the epithelium.

American Psychological Association (APA)

Vinciguerra, Paolo& Mencucci, Rita& Romano, Vito& Spoerl, Eberhard& Camesasca, Fabrizio I.& Favuzza, Eleonora…[et al.]. 2014. Imaging Mass Spectrometry by Matrix-Assisted Laser DesorptionIonization and Stress-Strain Measurements in Iontophoresis Transepithelial Corneal Collagen Cross-Linking. BioMed Research International،Vol. 2014, no. 2014, pp.1-12.
https://search.emarefa.net/detail/BIM-1034452

Modern Language Association (MLA)

Vinciguerra, Paolo…[et al.]. Imaging Mass Spectrometry by Matrix-Assisted Laser DesorptionIonization and Stress-Strain Measurements in Iontophoresis Transepithelial Corneal Collagen Cross-Linking. BioMed Research International No. 2014 (2014), pp.1-12.
https://search.emarefa.net/detail/BIM-1034452

American Medical Association (AMA)

Vinciguerra, Paolo& Mencucci, Rita& Romano, Vito& Spoerl, Eberhard& Camesasca, Fabrizio I.& Favuzza, Eleonora…[et al.]. Imaging Mass Spectrometry by Matrix-Assisted Laser DesorptionIonization and Stress-Strain Measurements in Iontophoresis Transepithelial Corneal Collagen Cross-Linking. BioMed Research International. 2014. Vol. 2014, no. 2014, pp.1-12.
https://search.emarefa.net/detail/BIM-1034452

Data Type

Journal Articles

Language

English

Notes

Includes bibliographical references

Record ID

BIM-1034452