The University of Tokyo

Otsuka Chemical Co., Ltd.

Technion Research & Development Foundation Limited

National Institutes of Health, a Component of the US Dept. of Health & Human Services

Osaka University

New England Biolabs, Inc.

Peptidream Inc.

Hiroaki Suga

Yuki Goto

Hiroshi Murakami

Jun Igarashi

Takashi Higuchi

Yusuke Yamagishi

Mickal Nawatha

Joseph Rogers

Ashraf Brik

Takashi Kawakami

Takayuki Katoh

Atsushi Ohta

Hiroyuki Noji

James Inglese

Patrick Reid

Clotilde K Carlow

Junichi Takagi

Zhiru Li

Yumi Ito

Patricia Dranchak

Takeo Iida

Yukiko Matsunaga

Hao Yu

Daishi Fujita

Rikiya Watanabe

Hiroyasu Onaka

Alexander Vinogradov

Nasir Kato Bashiruddin

Shotaro Tsunoda

Jumpei Morimoto

Kenichiro Ito

Ryan MacArthur

Takahiro Ishizawa

Yasuharu Kato

Hiroshi Ashigai

Yusuke Sako

The present invention provides a method for producing a compound library comprising two or more cyclic compounds represented by the formula (I), comprising a step of allowing a macrocyclase in vitro to act on two or more peptides represented by the formula (II): LP-X-(Xa)-Y-Z (II) wherein X represents a group represented by the formula (1), Y is a peptide residue consisting of four amino acids and/or analogs thereof and contains a group represented by the formula (2) (wherein Rand Bare as defined above, and Rrepresents a hydrogen or a hydrocarbon group), and LP is present or absent and, when present, represents a peptide residue consisting of 1 to 100 amino acids and/or analogs thereof, and forming the nitrogen-containing 6-membered ring A while eliminating LP, if present, to form the two or more cyclic compounds represented by the formula (I).

Compound library and method for producing compound library

The present invention is directed to a cyclic polypeptide having ubiquitin binding affinity (K) of 0.1-100 nM. Further provided are methods for reducing deubiquitination activity of a cell, and for treating cancer in a subject in need thereof.

Ubiquitin high affinity cyclic peptides and methods of use thereof

The present invention provides a Plexin-binding regulating agent containing a cyclic peptide having an Arg-Trp-Thr structure or a Leu-Ser-Trp structure or a pharmaceutically acceptable salt of the cyclic peptide.

Plexin binding regulator

The purpose of the present invention is to provide, for translation in a cell-free translation system, a novel translation system capable of synthesizing a peptide having therein consecutive non-proteinogenic amino acids. The present invention provides a tRNA containing the base sequence represented by SEQ ID NO: 1 and encoding a non-proteinogenic amino acid.

Modification of D- and T-arms of tRNA enhancing D-amino acid and β-amino acid uptake

Disclosed herein are isolated peptides inhibit activity of a cofactor-independent phosphoglycerate mutase. In some examples, the isolated peptide is 6-20 amino acids long and includes the amino acid sequence of any one of SEQ ID NOs: 1-22 or 54, an analog or derivative thereof, or a pharmaceutically acceptable salt or ester thereof. In some examples, the peptide is a cyclic peptide with an N-terminal ring of 6-15 amino acids (for example, 6-10 amino acids) and a C-terminal linear portion of 1-9 amino acids (for example, 3-8 amino acids. Also disclosed h are methods of treating or inhibiting an infection in a subject, including administering to the subject an effective amount of a composition including one of more of the disclosed peptides, or analogs or derivative thereof, or pharmaceutically acceptable salts or esters thereof.

Peptide inhibitors of phosphoglycerate mutase and methods of use

A material film is formed as a thin film having a thickness of 1 &#x3bc;m on a surface of a glass substrate. A plurality of micro-chambers having a diameter of 5 &#x3bc;m are formed in the material film to be arrayed at a high density. The respective chambers filled with an aqueous test solution have openings that are liquid-sealed by a lipid bilayer membrane to provide a high-density micro-chamber array. Significant downsizing of the micro-chambers enhances a change in concentration by a reaction of one biomolecule in the chamber and thereby increases the detection sensitivity. In the configuration that a large number of micro-chambers are formed at a high density, even in the case of an extremely slow reaction of the biomolecule, the reaction proceeds in any of the chambers. This configuration accordingly enables the reaction of the biomolecule to be detected with high sensitivity.

High-density microchamber array and manufacturing method thereof

An object of the invention is to provide a peptide having a stabilized secondary structure. The present invention provides a peptide having a secondary structure stabilized by a crosslinked structure and containing at least one combination of a special amino acid of the formula (I): (wherein, (A) represents a single bond or a linking group having, in the main chain thereof, from 1 to 10 atoms;(B) represents a group containing at least one &#x3c0; bond;(C) represents a hydrogen atom or an alkyl group which may be substituted with a substituent; and X represents a group substitutable by a substitution reaction with a sulfanyl group) and an amino acid having, in the side chain thereof, a sulfanyl group; and having the crosslinked structure formed through a thioether bond between the side chain of the special amino acid residue and the sulfanyl group.

Peptide with safer secondary structure, peptide library, and production methods for same

An object of the present invention is to provide a method of stably introducing a heterocycle into a substrate peptide by using an azoline backbone introducing enzyme. The present invention provides a method of introducing a heterocycle into a leader-sequence-free substrate peptide by using an azoline backbone introducing enzyme to which a leader sequence of the substrate has been bound.

Method for producing compound containing heterocycle

An object of the present invention is to provide a peptide excellent in resistance against metabolism, having a stable structure in vivo, and capable of penetrating a cell membrane and reaching in cells. The present invention provides a macrocyclic peptide having a macrocyclic structure comprised of four or more amino acids. At least two amino acids not adjacent to each other have a hydrophobic side chain and the hydrophobic side chains interact with each other inside the ring of the macrocyclic peptide in a hydrophilic environment.

Macrocyclic peptide, method for producing same, and screening method using macrocyclic peptide library

An object of the present invention is to provide a method of efficiently constructing a library abundant in diversity and also usable for screening of a compound that binds to a target substance having protease activity. The present invention provides a method of constructing an azoline compound library containing two or more azoline compounds having an azoline backbone introduced into at least one of Cys, Ser, Thr, and 2,3-diamino acid, and analogs thereof of Xaaof a peptide represented by the following formula (I):A-(Xaa)-B&#x2003;&#x2003;(I)[wherein, m numbers of Xaas respectively represent arbitrary amino acids, at least one of which is an amino acid selected from the group consisting of Cys, Ser, Thr, and 2,3-diamino acid, and analogs thereof, m represents an inter selected from 2 to 40, and A and B each independently represent a peptide composed of from 0 to 100 amino acids].

Azoline compound and azole compound library and method for producing same

Object is to provide a method of constructing a library of peptides having, at a desired position in the random sequence of each peptide, an amino acid having a portion capable of binding to a target. The invention provides a method of producing a library of peptides having, at a designated position in the random sequence of each peptide, a special amino acid having a portion capable of binding to a target, including (i) preparing a library of mRNAs having, in the mRNA sequence coding for a random amino acid sequence, a base sequence having an altered codon encoding the special amino acid, (ii) preparing an aminoacyl tRNA with the special amino acid linked to a tRNA encoded by the altered codon, and (iii) translating the mRNAs by using a cell-free translation system containing the aminoacyl tRNA to obtain a library of peptides having, in the random sequence thereof, a predetermined special amino acid.

Peptide library production method, peptide library, and screening method

A peptide functioning as a c-Met agonist is described. A peptide complex comprising two or more peptides that bind to a c-Met protein and a linker that links the two or more peptides to one another is described. Such a peptide complex promotes autophosphorylation of the c-Met protein and induces cell growth.

c-Met protein agonist

An object of the present invention is to provide a VEGFR2 inhibitor peptide having high specificity and available at a low cost. The present invention provides a peptide having the following amino acid sequence: [wherein, Xaarepresents Val or derivative thereof, Xaarepresents Asp or derivative thereof, Xaarepresents Pro or derivative thereof, Xaarepresents Trp or derivative thereof, Xaarepresents Asn or derivative thereof, Xaarepresents Gly or derivative thereof, Xaarepresents Leu or derivative thereof, Xaa, Xaato Xaa, Xaa, and Xaato Xaaeach independently represent an arbitrary amino acid or derivative thereof]; or [wherein, Xaarepresents His or derivative thereof, Xaarepresents Pro or derivative thereof, and Xaato Xaaand Xaato Xaaeach represent an arbitrary amino acid].

Peptide for inhibiting vascular endothelial growth factor receptor

Object of the present invention is to develop an artificial synthesis system of various peptides having an azole derivative structure and develop a library of such peptides. The present invention provides a method of producing a peptide having, in the backbone thereof, an azole derivative structure comprising the step of: synthesizing a substrate peptide of an azoline structure introducing enzyme having, in the modified region thereof, at least any one of the following amino acids, [in any of the compounds,

Method for producing peptides having azole-derived skeleton

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Tokyo, Japan

Hiroaki Suga