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429 results on '"Kobayashi, Kazukiyo"'

26. A quantitative estimation of carbohydrate-carbohydrate interaction using clustered oligosaccharides of glycolipid monolayers and of artifical glycoconjugate polymers by surface plasmon resonance

Author

Matsuura, Kazunori, Kitakouji, Hiromoto, Sawada, Naoki, Ishida, Hideharu, Kiso, Makoto, Kitajima, Ken, and Kobayashi, Kazukiyo

Subjects
Biochemistry -- Research, Cellular recognition -- Research, Oligosaccharides -- Research, Chemistry
Abstract

A new study uses surface plasmon resonance to investigate the carbohydrate-carbohydrate interaction using glycosphingolipids in Langmuir monolayers and glycoconjugate polystyrenes in water.

Published
2000

31. New development of cell adhesion system

Author

Kobayashi Kazukiyo, Akaike Toshihiro, and Kobayashi Akira

Subjects
World Wide Web, Engineering, Thesaurus (information retrieval), business.industry, business, Cell adhesion
Published
1994

32. Lactose-carrying polystyrene as a drug carrier: investigation of body distributions to parenchymal liver cells using 125I-labelled lactose-carrying polystyrene

Author

Kobayashi Akira, Tatsuki Shinoda, Chang Chia-Wun, Maeda Atsushi, Yura Hirohumi, Kobayashi Kazukiyo, Goto Mitsuaki, Kojima Seiki, and Akaike Toshihiro

Subjects
Dissociation constant, Kidney, medicine.anatomical_structure, Biochemistry, Chemistry, Asialoglycoproteins, Hepatocyte, medicine, Pharmaceutical Science, Asialoglycoprotein receptor, Drug carrier, Receptor, Small intestine
Abstract

Directed toward pharmacological applications of lactose-carrying polystyrene, (poly ( N-p- vinylben-zyl -O-β- d -galactopyranosyl-(1→ 4)- d -gluconamide ) , PVLA), its body distribution, clearance from blood and specific binding to receptors have been investigated using radiolabelled PVLA. 125I-Labelled PVLA was prepared via copolymerization of N-p- vinylbenzyl -O-β- d -galactopyranosyl-(1 → 4)- d -glu-conamide (VLA) with 10 mol% of 4-(2-propenyl)phenyl acetate followed by radiolabelling of the latter component. When 125I-labelled PVLA was injected into rats through their tail veins, the radio-activity was distributed highly to liver, less to thyroid gland, cecum-large intestine, urine, feces and blood, and much less to lung, heart, kidney, spleen, pancreas, small intestine and urinary bladder. Its concentration to liver was visible by whole-body autoradiography. It was clarified that about 97% of PVLA was distributed to parenchymal liver cells and only 3% to nonparenchymal liver cells. The radioactivity in blood was decreased with time according to a biexponential curve. A two open compartment model is proposed on the basis of the pharmacokinetic analysis of the equation, which elucidated that PVLA migrated rapidly from blood to parenchymal liver cells. Specific binding between 125I-labelled PVLA and asialoglycoprotein receptors on parenchymal liver cells was demonstrated by its inhibition with asialofetuin. The bond dissociation constant estimated by Scatchard analysis was Kd= 1.4 × 10−9 M. The binding was as strong as those of several naturally occurring asialoglycoproteins. These properties of PVLA, as liver-specific targeting materials using galactose ligands as recognition signals to asialoglycoprotein receptors, are discussed with the conformational structures of PVLA which can carry drugs in their hydrophobic regions.

Published
1994

34. A globotriaosylceramide (Gb_3Cer) mimic peptide isolated from phage display library expressed strong neutralization to Shiga toxins

Author

Miura, Yoshiko, Sakaki, Akio, Kamihira, Masamichi, Iijima, Shinji, Kobayashi, Kazukiyo, Miura, Yoshiko, Sakaki, Akio, Kamihira, Masamichi, Iijima, Shinji, and Kobayashi, Kazukiyo

Abstract

A Gb_3-trisaccharide mimic peptide was selected with biopanning from a phage display library against anti-Gb_3 antibody to neutralize Shiga toxins (Stxs). Biopanning was carried out on a microplate immobilized with a Fab fragment of anti-Gb_3 antibody and a subtraction procedure screening was applied to enhance specificity. The selected phage clones showed strong affinity to anti-Gb_3 antibody and to Stxs. Among these clones, a 9-mer sequence WHWTWLSEY was determined as the strongest Gb_3 mimic peptide and chemically synthesized. The peptide bound strongly to Stx-1 and Stx-2, though the binding was inhibited with Gb_3Cer. Surface plasmon resonance (SPR) and fluorescent spectroscopy determined that the affinity of the peptide to both Stxs was strong. Neutralization activity was confirmed by in vitro assay with HeLa cells. The Gb_3 mimic peptide potentially has great promise for use against Stxs., identifier:https://dspace.jaist.ac.jp/dspace/handle/10119/4953

Published
2006

35. Peptides binding to a Gb3 mimic selected from a phage library

Author

Miura, Yoshiko, Sasao, Yuuki, Kamihira, Masamichi, Sakaki, Akio, Iijima, Shinji, Kobayashi, Kazukiyo, Miura, Yoshiko, Sasao, Yuuki, Kamihira, Masamichi, Sakaki, Akio, Iijima, Shinji, and Kobayashi, Kazukiyo

Abstract

Peptides binding to a Gb3 mimic were selected from 12mer peptide library. The self-assembled monolayer (SAM) of a Gb3 mimic was formed on the gold surface, and biopanning was carried out with the phage display peptide library. After 3 rounds of biopanning, four individual sequences were obtained from 10 phage clones, and the selected peptides having the specific 7mer sequence (FHENWPS) showed affinities to the Gb3 mimic as strong as to RCA_<120>. Molecular dynamics calculations suggested that the peptides bound to the Gb3 mimic by hydrophobic interaction and hydrogen bonding formation, and the cooperative interactions played an important role in the recognition. The Stx-1 binding was inhibited by the peptides., identifier:https://dspace.jaist.ac.jp/dspace/handle/10119/4945

Published
2004

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