Abstract: The object of the present invention is to provide a method for manufacturing an amino acid polymer more simply and efficiently compared to conventional methods for manufacturing amino acid polymers. The present invention provides a method for manufacturing an amino acid polymer with thioacid amino acids. Specifically, the manufacturing method of the present invention comprises (A) a step of preparing first and second thioacid amino acids, (B) a step of subjecting said first and second thioacid amino acids to an oxidation reaction to obtain an amino acid polymer linked by peptide bonds. The manufacturing method of the present invention is characterized in that it partially uses thioacid amino acids that do not possess a protecting group.

Abstract: An object of the invention is to provide a method of uniformly and efficiently producing a saccharide having a sulfate group and/or a phosphate group in the molecule, or a compound containing the saccharide. [Solution] The present invention provides a method of producing a saccharide having a sulfate group and/or a phosphate group. The method comprises (a) a step of preparing a “first saccharide having a non-protected sulfate group and/or a non-protected phosphate group” and a “second saccharide having a non-protected sulfate group and/or a non-protected phosphate group” and (b) a step of condensing the first saccharide and the second saccharide prepared in the step (a) with each other.

Abstract: An object of the present invention is to provide an albumin-sugar chain complex bound with a number of sugar chains sufficient for obtaining a sugar chain clustering effect while also being able to exist comparatively stably in the body. The present invention provides an albumin-sugar chain complex having five or more molecules of an asparagine-linked sugar chain bound per molecule of albumin; a carrier for selectively delivering a functional molecule to a target tissue in the body that contains the aforementioned albumin-sugar chain complex; and a bioimaging probe having the aforementioned albumin-sugar chain complex as an active ingredient thereof that is administered into the body of an animal.

Abstract: The object of the present invention is to provide a glycosylated polypeptide having uniform sugar chain structure which has interferon ? activity. It was found that a glycosylated polypeptide having uniform sugar chain structure as well as having interferon ? activity can be prepared by a method comprising a step of synthesizing a glycosylated peptide fragment and at least two peptide fragments and a step of linking the glycosylated peptide fragment and the at least two peptide fragments.

Abstract: To provide a carrier linker that is capable of improving the water solubility of a physiologically active substance and more quickly releasing the physiologically active substance under specific conditions without utilizing light or enzymatic cleavage. [Solution] A novel sugar chain-attached linker comprising a sugar chain that is attached as a carrier.

Abstract: The object of the present invention is to provide a polypeptide having interferon ? activity glycosylated with highly uniform sialylated sugar chains. The present invention is a glycosylated polypeptide, wherein the polypeptide is any polypeptide selected from the group consisting of the following (1) to (4); (1) a polypeptide consisting of the amino acid sequence represented by SEQ ID NO. 1, (2) a polypeptide having one or a few amino acids deleted, substituted, or added in the polypeptide consisting of the amino acid sequence represented by SEQ ID NO. 1, (3) a polypeptide that is an analog of interferon ?, and (4) a polypeptide having 80% or more homology to the polypeptide consisting of the amino acid sequence represented by SEQ ID NO. 1, in which amino acids at 4 to 6 locations are substituted with glycosylated amino acids, and wherein all of the non-reducing terminals of said sugar chain are sialylated.

Abstract: The object of the present invention is to provide a method of efficiently manufacturing an optically active D- and/or L-form amino acid possessing a thiol group in the side chain by a simple method. The present invention provides a method of manufacturing an amino acid derivative possessing a thiol group in the side chain, characterized in manufacturing an intermediate composition comprising D- and L-forms of an amino acid derivative possessing a thiol group at the ?-position, reacting a hydrolase selective for D- or L-amino acids, and separating the hydrolyzed D- or L-amino acid derivative, as well as an intermediate thereof.

Abstract: An object of the present invention is to provide an albumin-sugar chain complex bound with a number of sugar chains sufficient for obtaining a sugar chain clustering effect while also being able to exist comparatively stably in the body. The present invention provides an albumin-sugar chain complex having five or more molecules of an asparagine-linked sugar chain bound per molecule of albumin; a carrier for selectively delivering a functional molecule to a target tissue in the body that contains the aforementioned albumin-sugar chain complex; and a bioimaging probe having the aforementioned albumin-sugar chain complex as an active ingredient thereof that is administered into the body of an animal.

Abstract: The object of the present invention is to provide a sugar chain-polypeptide complex that may form a transparent and homogeneous hydrogel in a broad pH. The present invention provides a sugar chain-polypeptide complex, characterized in that said polypeptide is a polypeptide comprising an amino acid sequence consisting of 8-34 amino acid residues in which polar and nonpolar amino acid residues are alternately arranged, and one or more sugar chains are bound to said polypeptide.

Abstract: [Problem] To provide a glycosylated polypeptide having an affinity to somatostatin receptors, and, compared to somatostatins, having improved in-blood stability. [Solution] The glycosylated polypeptide is characterized by at least one amino acid in a somatostatin or an analog thereof being replaced with a glycosylated amino acid.

Abstract: When manufacturing a sugar chain compound having an activating group, there was a problem with the ammonium carbonate method that is the conventional technology that during the process of introducing an amino group at the reducing terminal of the sugar chain, the unit sugar located at the reducing terminal of the sugar chain is subjected to ring-opening, thus causing a mixture of ? and ? anomers to be produced.

Abstract: [Problem] To provide a glycosylated polypeptide having affinity to somatostatin receptors and, compared to somatostatins, having improved in-blood stability. [Solution] The glycosylated polypeptide is characterized by at least two amino acids in a somatostatin or an analog thereof being replaced by glycosylated amino acids.

Abstract: [Problem to be Solved] The importance of sugar chains having ?2,3- or ?2,6-linked sialic acid at their non-reducing ends is known. Industrial production has been demanded for these sugar chain compounds. Particularly, the production of glycoprotein drugs or the like inevitably requires producing in quantity sugar chains having homogeneous structures by controlling the linking pattern (?2,6-linkage or ?2,3-linkage) of sialic acid. Particularly, a triantennary or tetraantennary N-type complex sugar chain having sialic acid at each of all non-reducing ends is generally considered difficult to chemically synthesize. There has been no report disclosing that such a sugar chain was chemically synthesized. Furthermore, these sugar chains are also difficult to efficiently prepare enzymatically.

Abstract: [Problem] The purpose is to provide a compound containing a carrier linker moiety and a physiologically active substance moiety or a salt of the compound, wherein a carrier in the carrier linker moiety is biodegradable and is soluble in water. [Solution] The purpose can be achieved by employing a sugar chain as a carrier and focusing on the structure of a carrier-linker having a specified structure. A compound containing a carrier linker moiety and a physiologically active substance moiety or a salt of the compound is discovered.

Abstract: [Problem] To provide a glycosylated polypeptide having affinity to somatostatin receptors and, compared to somatostatins, having improved in-blood stability. [Solution] The glycosylated polypeptide is characterized by at least two amino acids in a somatostatin or an analogue thereof being replaced by glycosylated amino acids.

Abstract: [Problem] To provide a glycosylated polypeptide having an affinity to somatostatin receptors, and, compared to somatostatins, having improved in-blood stability. [Solution] The glycosylated polypeptide is characterized by at least one amino acid in a somatostatin or an analog thereof being replaced with a glycosylated amino acid.

Abstract: [Problem to be Solved] The importance of sugar chains having ?2,3- or ?2,6-linked sialic acid at their non-reducing ends is known. Industrial production has been demanded for these sugar chain compounds. Particularly, the production of glycoprotein drugs or the like inevitably requires producing in quantity sugar chains having homogeneous structures by controlling the linking pattern (?2,6-linkage or ?2,3-linkage) of sialic acid. Particularly, a triantennary or tetraantennary N-type complex sugar chain having sialic acid at each of all non-reducing ends is generally considered difficult to chemically synthesize. There has been no report disclosing that such a sugar chain was chemically synthesized. Furthermore, these sugar chains are also difficult to efficiently prepare enzymatically.

Abstract: A process for chemically converting a peptide chain into a peptide thioester includes, when a —C(?X)—R1 group is introduced to the thiol group of the cysteine residue and then the resulting peptide is reacted with a compound having a leaving group represented by the formula: —NH—C(?Y)NHR3 in an organic solvent, the —NH—C(?Y)NHR3 group binds via addition reaction to the carboxyl group of the N-terminal-side peptide bond of the cysteine residue, whereby the peptide bond is cleaved and the C-terminal-side peptide fragment is cut off. Further, when the resulting peptide chain having the —NH—C(?Y)NHR3 group is reacted with a thiol in a buffer solution, a thiol exchange reaction occurs, namely, the thiol group of the thiol binds to the carbonyl carbon to which the —NH—C(?Y)NHR3 group has bound, whereby the —NH—C(?Y)NHR3 group is eliminated.

Abstract: [Technical Problem] To provide a method for manufacturing that enables to obtain a targeted glycopeptide harboring a sialyl sugar chain in high yield without decomposing sialic acid at a non-reducing terminal of sugar chain when the glycopeptide is synthesized by a Boc solid phase synthesis method. [Solution to Problem] The present invention is characterized in that the Boc-sialylglycosylated amino acid derivative used in Boc solid phase synthesis method is one where the carboxyl group of the sialic acid at the sugar chain non-reducing terminal is protected with a phenacyl group.

Abstract: A method for efficiently manufacturing a polypeptide fragment suitable for the NCL method includes a step of reacting a polypeptide containing a first polypeptide fragment having cysteine at the N-terminal and a second polypeptide fragment linked via an intervening sequence -Cys-W-(His)n-Z-Met- with CNBr to obtain a first polypeptide fragment having cysteine at the N-terminal and a third polypeptide fragment, and a step of sequentially reacting the third polypeptide fragment with a compound represented by the following formula (I) and a compound represented by the following formula (II) to obtain a second polypeptide fragment having the C-terminal modified.