Relative Peripheral Myopia Induced by Fractal Contact Lenses.

PURPOSE: To assess the peripheral refraction induced by Fractal Contact Lenses (FCLs) in myopic eyes by means of a two-dimensional Relative Peripheral Refractive Error (RPRE) map. MATERIALS AND METHODS: This study involved 26 myopic subjects ranging from -0.50 D to -7.00 D. FCLs prototypes were custom-manufactured and characterized. Corneal topographies were taken in order to assess correlations between corneal asphericity and lens decentration. Two-dimensional RPREs were measured with an open-field autorefractor at 67 points, covering the central 60 × 30 degrees of the visual field. The bidimensional RPRE vector components: M, J0 and J45 of the difference between the values obtained with and without the FCLs in the eye were obtained. Additionally, the FCL-induced peripheral refraction in tangential and sagittal planes was computed along the horizontal meridian. RESULTS: Induced by the FCLs, significant differences for all vector components were found in the peripheral retina. FCLs were decentered a mean of 0.7 ± 0.19 mm to the temporal cornea. The two-dimensional RPRE maps manifested the FCLs decentration. In particular, M varied asymmetrically between nasal and temporal retina after fitting the FCLs with a significant increment of the myopic shift beyond 10º (p < 0.05). No correlations were found between the amount of lens decentration and the asphericity of the cornea along temporal and nasal sides. However, significant correlations were found between the corneal asphericity and vector components of the RPRE in naked eyes. FCLs produced an increasing myopic shift in tangential and sagittal power errors along the horizontal meridian. CONCLUSIONS: As predicted by ray-tracing simulations, FCLs fitted in myopic eyes produce a myopic shift of the RPRE. The two-dimensional RPRE maps show information about the lens performance that is hidden in the conventional one-dimensional meridional representations.

The Monkey King: a personal view of the long journey towards a proteomic Nirvana.

The review covers about fifty years of progress in "proteome" analysis, starting from primitive two-dimensional (2D) map attempts in the early sixties of last century. The polar star in 2D mapping arose in 1975 with the classic paper by O'Farrell in J Biol. Chem. It became the compass for all proteome navigators. Perfection came, though, only with the introduction of immobilized pH gradients, which fixed the polypeptide spots in the 2D plane. Great impetus in proteome analysis came with the introduction of informatic tools and creating databases, among which Swiss Prot remains the site of excellence. Towards the end of the nineties, 2D chromatography, epitomized by coupling strong cation exchangers with C18 resins, began to be a serious challenge to electrophoretic 2D mapping, although up to the present both techniques are still much in vogue and appear to give complementary results. Yet the migration of "proteomics" into the third millennium was made possible only by mass spectrometry (MS), which today represents the standard analytical tool in any lab dealing with proteomic analysis. Another major improvement has been the introduction of combinatorial peptide ligand libraries (CPLL), which, when properly used, enhance the visibility of low-abundance species by 3 to 4 orders of magnitude. Coupling MS to CPLLs permits the exploration of at least 8 orders of magnitude in dynamic range on any proteome. BIOLOGICAL SIGNIFICANCE: The present review is a personal recollection highlighting the developments that led to present-day proteomics on a long march that lasted about 50years. It is meant to give to young scientists an overview on how science grows, which ones are the quantum jumps in science and which research is of particular significance in general and in the field of proteomics in particular. It also gives some real-life episodes of greater-than-life figures. As such, it can be viewed as a tutorial to stimulate the young generation to be creative (and use their imagination too!).This article is part of a Special Issue entitled: 20years of Proteomics in memory of Viatliano Pallini. Guest Editors: Luca Bini, Juan J. Calvete, Natacha Turck, Denis Hochstrasser and Jean-Charles Sanchez.