Shimadzu Corporation

Hipep Laboratories

Nippon Light Metal Company, Ltd.

Nokihara, Kiyoshi

Kiyoshi Nokihara

Rintaro Yamamoto

Yasuo Oka

Shin Nakamura

Makoto Hazama

Yasushi Takebayashi

Akiyoshi Hirata

Atsushi Kitagawa

Mitsuhiro Hashimoto

Yoshiyuki Togawa

Naoki Morita

Hisakazu Mihara

Shun Nokihara

Koji Muramoto

Masaki Noda

Michael Kiffe

Yuki Tominaga

Disclosed are a novel compound having a higher angiogenic effect than that of a known peptide-based angiogenic agent, and an angiogenic agent including the novel compound. The compound is represented by the following formula [1]: Cyclic(Cys-O2Oc-SVV(F/Y)GLRG-Cys)-NH(wherein the number of oxyethylene units, represented by O2Oc, is within the range of 2 to 6), the following formula [II]: Cyclic(OOc-SVV(F/Y)GLRQ)-NH[II] (wherein the number of oxyethylene units, represented by O2Oc, is within the range of 2 to 6), or the following formula [III]: OOc-SVV(F/Y)GLR-NH[III] (wherein the number of oxyethylene units, represented by O2Oc, is within the range of 2 to 6).

Compound and angiogenic agent comprising same

A substrate for biochips which has a high probe loading amounts and a uniform immobilization density, and which further has a high detection sensitivity and a high reproducibility by preventing a non-specific adsorption of proteins, when used as a substrate for biochips for immobilizing probes composed of biologically relevant substances such as proteins and nucleic acids, is disclosed. Amino groups can be bound to the surface of the substrate uniformly, at a high density and stably by covalently immobilizing an amino group-containing polymer on the surface of the substrate. The probe immobilization rate is high and immobilizing density was uniform by immobilizing a probe composed of a biologically relevant substance such as a protein or nucleic acid by utilizing the amino groups. Further, detection sensitivity and reproducibility are high by inhibiting non-specific adsorption of proteins.

Biochip substratum and method for production thereof

A biochip substrate which is free from cross-contamination due to spot spreading or contact with spots adjacent to each other, and a biochip using the same. A biochip substrate on which multiple valleys for immobilizing biological substances are formed so as to prevent cross-contamination due to spot spreading or contact with spots adjacent to each other, and a biochip using the same are provided. Moreover, it is found out that a desired binding in a target molecule contained in a test sample occurs at a detectable level in a solution system even in the case where a valley have such a small capacity as 1 nL to 10 nL.

Biochip substrate and biochip

A substrate for biochips with which immobilization is easy, which does not exhibit self-fluorescence, which is easy to manufacture, and which is excellent in flatness and surface precision, is disclosed. A substrate having a substrate body of the biochip, which is made of a metal, and a carbon layer having functional groups formed on the metal substrate body is used as a substrate for biochips. Since the substrate body of the substrate for biochips is made of a metal, the substrate is not only easy to manufacture, but also free from cracking and chipping, so that it allows easy handling, and high flatness and surface precision can be attained. Therefore, the problem that the optical system is hard to focus when detecting fluorescence does not occur. Moreover, since the substrate body is made of a metal, it does not emit fluorescence by itself. In addition, since the carbon layer has functional groups such as amino groups, biologically relevant substances can be easily immobilized.

Substrate for biochip and biochip

Disclosed is a peptide-immobilized substrate for measuring a target protein, with which the peptide can have a structure required for being recognized by the target protein, with which the accurate loading amount of the peptide can be attained, and by which a trace amount of the target protein may be measured accurately and simply. The peptide-immobilized substrate for measuring a target protein according to the present invention comprises a chemically synthesized peptide having an expected spatial structure or having a binding ability with the target protein, which peptide can bind with the target protein and is immobilized on the substrate.

Peptide-immobilized substrate and method for measuring target protein

Means for overcoming the problems which the conventional glass microchannel chips have are disclosed. That is, a microchannel chip in which microchannels can be formed at a low cost, and which has a high chemical resistance is disclosed. The microchannel chip is constituted by a substrate made of carbon, which has a channel in its surface; and a cover composed of a glass plate bonded to the substrate. The cover is bonded to the substrate by heating at least a part of the contact surface at which the substrate is in contact with the cover.

Micro-passage chip

A method for recovering an optically pure amino acid derivative from a waste liquor collected after a coupling reaction in peptide synthesis, comprising the steps of (a) adding into the waste liquor, in which an uncoupled amino acid derivative or an uncoupled small peptide fragment is contained, a compound selected from the group consisting of 1-hydroxybenzotriazole (HOBt), 1-hydroxy-7-azabenzotriazole (HOAt), 3-hydroxy-4-oxo-3,4-dihydro-1,2,3-benzotriazine (HOObt) and N-hydroxy-5-norbornen-2,3-dicarboxylic acid imide(HONB); (b) concentrating the waste liquor obtained in step (a); (c) treating a residue obtained in step (b) with an acidic buffer solution containing a tertiary amine; and (d) extracting and purifying the uncoupled amino acid derivative or the uncoupled small peptide fragment under acidic conditions.

Method for recovering optically pure amino acid derivatives

The present invention relates to a method for peptide C-terminal fragment sequence analysis, in which the fragment collection is carried out on an allylamine group-derivatized polymer membrane or on allylamine group-derivatized glass fiber filter paper; the collected C-terminal fragment is immobilized thereon using a water-soluble carbodiimide etc.; and the obtained immobilized product is subjected directly to amino acid sequence analysis. The present invention also relates to an apparatus for collecting a peptide fragment. According to the method of the present invention, peptides which are rich in hydrophobic groups in their C-terminus and are therefore difficult to trap with polyvalent ion carriers, currently used in the gas-phase sequencer, can be completely analyzed up to their C-terminus. Also, amino acid sequence analysis can be made even when the amount of C-terminal fragments is very small. In addition, since collection and immobilization of fragments can be done in the same bottle, the risks of contamination and mechanical loss are very low.

Method for peptide C-terminal fragment sequence analysis and apparatus

A cleavage apparatus for obtaining a free peptide after assembly of a peptide on a solid support by solid-phase peptide synthesis equipped with a cleavage cocktail transport line installed between the column for cleavage containing a peptidyl resin and a cleavage cocktail supply bottle, through which a cleavage cocktail is supplied from the bottle to the column and recovered into the cleavage cocktail supply bottle from the column. This apparatus can provide easy, safe, rapid and reliable cleavage in a large scale peptide synthesis.

Cleavage apparatus

The present invention is directed to a compound represented by the following formula (I), ##STR1## and a linker for peptide synthesis using the above compound. When the linker of the present invention is used for the solid-phase peptide synthesis, it is possible to synthesize those peptides which are sensitive to acid and difficult to synthesize by conventional methods. Also, side reactions can be prevented, and the desired product is produced at a high purity because cleavage can be achieved under milder conditions or in shorter times. In other words, efficient peptide synthesis is possible.

Dibenzosuberyl and dibenzosuberenyl derivatives

The present invention relates to an apparatus for collecting a peptide fragment, wherein a C-terminal peptide fragment is collected from a peptide fragment mixture resulting from specific cleavage of the peptide bond between a lysine residue and the C-terminal amino acid residue adjacent thereto. The apparatus has an immobilizing means, a cleaving means, a recovering means and a control means. According to the present invention, since the control means sequentially executes the immobilizing means, cleaving means and recovering means, no skillful work is required in peptide fragment collection, making it possible to collect the carboxyl-terminal peptide fragment with simple operation and high reproducibility.

Apparatus for collecting peptide fragment

The present invention is directed to a simultaneous multiple chemical synthesizer comprising a number of reaction vessels wherein each vessel has a filter in the bottom portion thereof, a number of needles wherein each needle is connected to an aspiration injection line of a reaction mixture and a gas supply line in connection with each reaction vessel and each needle does not touch the resin contained in the reaction vessel, a number of arms which are horizontally and vertically movable and hold the respective needles, a bubbling gas line and a waste discharge line in connection with each reaction vessel, wherein each line is connected to the bottom portion of each reaction vessel, a number of purging means which move synchronously with said waste discharge lines, and means for washing the portions of the needles and purge means which contact with the reaction reagents.

Simultaneous multiple chemical synthesizer

The present invention is directed to an automated peptide synthesizer equipped with recovery lines including an acyl component recovery line for recovering unreacted acyl components to allow the reuse of the acyl components, and a solvent recovery line for recovering and distilling a reaction solvent and passing it through a purification column to allow the reuse of the reaction solvent. Both recovery lines are installed on the flow pathway from one or more reaction chambers or columns to a waste liquid reservoir of the automated peptide synthesizer. By recovering expensive acyl components and solvents, running cost in peptide synthesis can be reduced to mitigate economic burden, and the amount of waste leading to environmental destruction can be reduced.

Automated peptide synthesizer

In connection with an automated peptide synthesizer, an apparatus and associated method through which peptides produced in simultaneous multiple synthesis are together isolable. Cleavage to liberate the peptides from linkage to the support matrix of the solid phase is carried out in the same vessels in which the synthesizing reactions took place. Prior to cleavage, a drainage port of each reaction vessel is closed off by a cap. The reaction vessel is inserted into a centrifuge tube, which in turn is put into a rack supporting a number of tubes equal to the number of channels of the peptide synthesizing apparatus. After the peptides are cleaved and dissolved into cleaving solution added into each of the reaction vessels, the caps are removed from the drainage ports of each reaction vessel, and the vessel is returned into the centrifuge tube. A plastic jet-fitting attached to the nozzle tip of a blow unit pressure gun is inserted into and pressed into contact against the supply opening of the reaction vessel. Operating a trigger of the pressure gun releases pressurized inert gas into the reaction chamber. The peptide-dissolved cleaving solution is thereby passed through the drainage port, and is thus transferred in liquid phase into the centrifuge tube as filtrate. Associated with the blow unit pressure gun, a needle tube fitting is provided for localized desiccation of wetted peptide following precipitation and centrifuging.

Growing community of inventors

Kyoto, Japan

Kiyoshi Nokihara