Misalignment of center of foveal avascular zone and center of photoreceptors in eyes with history of retinopathy of prematurity.

To determine the relationship between the center of the foveal avascular zone (FAZ) and the center of the foveal photoreceptors in eyes with a history of retinopathy of prematurity (ROP). To accomplish this, we reviewed the medical records of patients with ROP who were examined at the ROP Clinic of the Tokyo Women's Medical University Hospital. We studied 43 eyes of 23 children with ROP and 67 eyes of 36 control children without any fundus abnormalities. The optical coherence tomography angiographic (OCTA) en face images were used to measure the size and location of the foveal avascular zone (FAZ), and cross-sectional OCT images to measure the central retinal thickness (CRT). Our results showed that the size of the FAZ was significantly smaller in the ROP group (0.200 ± 0.142 mm2) than in the control group (0.319 ± 0.085 mm2; P < 0.01). The CRT was significantly thicker in the ROP group (228 ± 30 µm) than in the control group (189 ± 13 µm; P < 0.01). The mean length of the foveal bulge was not significantly different between the two groups. The actual distance of the misalignment between the center of the FAZ and the center of the photoreceptors was significantly greater in the ROP group (50.4 ± 29.5 µm) than in the control group (39.6 ± 21.9 µm; P = 0.001). The correlations between the actual distance of misalignment and the size of the FAZ, CRT, and length of the foveal bulge in both groups were not significant. Despite the significant misalignment in eyes with a history of ROP, the center of the foveal photoreceptors was consistently located within the narrow FAZ which indicates that the development of the FAZ and photoreceptor formation are interrelated.

Foveal abnormalities determined by optical coherence tomography angiography in children with history of retinopathy of prematurity.

PURPOSE: To describe the foveal characteristics of children with a history of retinopathy of prematurity (ROP) using optical coherence tomography angiography (OCTA). METHODS: All eyes were examined by OCTA (RTVue AVANTI, Optovue Inc, Fremont, CA) with a scan of 3 × 3 mm cantered on the fovea. The size of the foveal avascular zone (FAZ), central retinal thickness (CRT), and foveal bulge were measured. RESULTS: Forty-eight eyes of 26 children with a history of ROP and a mean age of 8.8 years with a range of 4-16 years (ROP group) were studied. Sixty-six eyes of 36 children without any fundus abnormalities and with an average age of 10.5 years and a range of 3-17 years (control group) were studied as controls. The mean FAZ area in the ROP group was 0.18 mm2 which was significantly smaller than the 0.32 mm2 in the control group (p < 0.01). The mean CRT was significantly thicker in the ROP group (228 µm) compared to the control group (189 µm; p < 0.01). The size of FAZ was not measurable in 5 eyes (10.4%) of 3 children in the ROP group. The correlation between the FAZ area and CRT was significant in both the ROP and control groups (r = -0.53 in ROP; r = -0.57 in control; both p < 0.01). There was no significant difference in the height of the foveal bulge between two groups (p = 0.64). CONCLUSIONS: The FAZ is smaller in ex-preterm children with a history of ROP (including laser treatment for ROP) than in children who were not premature.

Efficient one-cycle affinity selection of binding proteins or peptides specific for a small-molecule using a T7 phage display pool.

Here, we report an efficient one-cycle affinity selection using a natural-protein or random-peptide T7 phage pool for identification of binding proteins or peptides specific for small-molecules. The screening procedure involved a cuvette type 27-MHz quartz-crystal microbalance (QCM) apparatus with introduction of self-assembled monolayer (SAM) for a specific small-molecule immobilization on the gold electrode surface of a sensor chip. Using this apparatus, we attempted an affinity selection of proteins or peptides against synthetic ligand for FK506-binding protein (SLF) or irinotecan (Iri, CPT-11). An affinity selection using SLF-SAM and a natural-protein T7 phage pool successfully detected FK506-binding protein 12 (FKBP12)-displaying T7 phage after an interaction time of only 10 min. Extensive exploration of time-consuming wash and/or elution conditions together with several rounds of selection was not required. Furthermore, in the selection using a 15-mer random-peptide T7 phage pool and subsequent analysis utilizing receptor ligand contact (RELIC) software, a subset of SLF-selected peptides clearly pinpointed several amino-acid residues within the binding site of FKBP12. Likewise, a subset of Iri-selected peptides pinpointed part of the positive amino-acid region of residues from the Iri-binding site of the well-known direct targets, acetylcholinesterase (AChE) and carboxylesterase (CE). Our findings demonstrate the effectiveness of this method and general applicability for a wide range of small-molecules.