[Impact of Aperture Shape Controller on Knowledge-based VMAT Planning of Prostate Cancer].

PURPOSE: Knowledge-based planning (KBP) has disadvantages of high monitor unit (MU) and complex multi-leaf collimator (MLC) motion. We investigated the optimal aperture shape controller (ASC) level for the KBP to reduce these factors in volumetric modulated arc therapy (VMAT) for prostate cancer. METHODS: The KBP model was created based on 51 clinical plans (CPs) of patients who underwent the VMAT for prostate cancer. Another 10 CPs were selected randomly, and the KBPs with/without ASC, changed stepwise from very low (KBP-VL) to very high (KBP-VH), were performed with a single auto-optimization. The parameters of dose-volume histograms (DVHs) and MLC performance metrics were evaluated. We obtained the modulation complexity score for VMAT (MCSv), closed leaf score (CLS), small aperture score (SAS), leaf travel (LT), and total MU. RESULTS: The ASC did not affect the DVH parameters negatively. The following comparisons of MLC performance were obtained (KBP vs. KBP-VL vs. KBP-VH, respectively): 0.25 vs. 0.27 vs. 0.30 (MCSv), 0.19 vs. 0.18 vs. 0.16 (CLS), 0.50 vs. 0.45 vs. 0.40 (SAS10 mm), 0.73 vs. 0.68 vs. 0.63 (SAS20 mm), 768.35 mm vs. 671.50 mm vs. 551.32 mm (LT), and 672.87 vs. 642.36 vs. 607.59 (MU). There were significant differences between KBP and KBP-VH for MCSv and LT (p<0.05). CONCLUSIONS: The KBP using an ASC set to the very high level could reduce the complexity of MLC motion significantly more without deterioration of the DVH parameters compared with the KBP in VMAT for prostate cancer.

AJIPHASE®: A Highly Efficient Synthetic Method for One-Pot Peptide Elongation in the Solution Phase by an Fmoc Strategy.

We previously reported an efficient peptide synthesis method, AJIPHASE®, that comprises repeated reactions and isolations by precipitation. This method utilizes an anchor molecule with long-chain alkyl groups as a protecting group for the C-terminus. To further improve this method, we developed a one-pot synthesis of a peptide sequence wherein the synthetic intermediates were isolated by solvent extraction instead of precipitation. A branched-chain anchor molecule was used in the new process, significantly enhancing the solubility of long peptides and the operational efficiency compared with the previous method, which employed precipitation for isolation and a straight-chain aliphatic group. Another prerequisite for this solvent-extraction-based strategy was the use of thiomalic acid and DBU for Fmoc deprotection, which facilitates the removal of byproducts, such as the fulvene adduct.

Cell- and region-specific expression of sugar chains in the mouse epididymal epithelium using lectin histochemistry combined with immunohistochemistry.

To understand the cytochemical properties of epididymal epithelial cells, the characteristics of glycoconjugates in the mouse epididymis were examined using the technique of lectin histochemistry combined with immunohistochemistry. Characteristic staining patterns depending on the type of lectins were observed in the epididymal epithelium. Principal cells expressed N-acetyl-D-galactosamine (GalNAc), N-acetyl-D-glucosamine (GlcNAc), and Fucose in the proximal region of the epididymis and Mannose, Glucose, and Galactose in the distal region of the epididymis. Basal cells expressed Mannose, Glucose, Galactose, and GlcNAc in the proximal region and Galactose in the distal region. On the other hand, clear cells expressed various sugar residues and differences among regions were not observed. Interestingly, principal cells, clear cells, and basal cells specifically reacted with Ulex Europaeus-Agglutinin I (UEA-I lectin), Maackia Amurensis-Lectin I (MAL-I lectin), and Griffonia simplicifolia Lectin I-B4 (GS-I B lectin), respectively. These findings indicate that the selectivity in lectin reactivity for distinct cell types and segment-dependent staining in the epididymis may be related to cellular and regional differences in function. Furthermore, because some lectins stain particular cells or cellular compartments selectively, these lectins could be useful markers for histopathological evaluation of diseases or diagnosis of male infertility.

Changes in lectin-binding sites on epididymal cells during postnatal development of the mouse.

Using lectin histochemistry combined with immunohistochemistry, we recently demonstrated that the principal, clear, and basal cells in the adult mouse epididymis specifically react with UEA-I, MAL-I, and GS-IB lectins, respectively. The present study examined the distribution of the lectin-binding sites for some lectins on the epididymal epithelium during postnatal development. Galactose staining with GS-IB was first detected in some of the undifferentiated epithelial cells in mice aged 1 week, and this characteristic became specific to basal cells in mice aged 2 weeks and above. Fucose staining with UEA-I was first detected in the principal cells in mice aged 3 weeks. Staining of sialic acid with MAL-I was first detected in all undifferentiated epithelial cells in mice aged 1 week, and this characteristic became specific to the narrow and clear cells in all regions and to the principal cells in regions IV and V in mice aged 3 weeks. The results indicate that epididymal differentiation is characterized by the expression of cell- and region-specific sugar chains that appear early during postnatal development before the sperm arrives in the epididymis.

Novel diphenylmethyl-derived amide protecting group for efficient liquid-phase peptide synthesis: AJIPHASE.

An efficient method for the synthesis of peptides bearing an amide at the C-terminal is described. This method involves the attachment of a C-terminal protecting group bearing long aliphatic chains, followed by the repetition of simple reaction and precipitation steps with the combined advantages of liquid-phase peptide synthesis (LPPS) and solid-phase peptide synthesis (SPPS). Using this method, a hydrophobic peptide was successfully synthesized in good yield and high purity, which cannot be obtained satisfactorily by SPPS.