Abstract: 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.

Abstract: The present invention relates to a cyclic peptide having a structure represented by the following formula (1): (in the formula (1), Xaa1 is a basic amino acid, Xaa2 is an amino acid, Xaa3 and Xaa4 are each independently a basic amino acid or an aromatic amino acid, and n1 is an integer of 0 to 10), or a pharmacologically acceptable salt of the cyclic peptide.

Abstract: The present invention is directed to a cyclic polypeptide having ubiquitin binding affinity (KD) 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.

Abstract: Described herein, inter alia, are Ras inhibitors and uses thereof.

Abstract: The present invention is directed to a cyclic polypeptide having ubiquitin binding affinity (KD) 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.

Abstract: The purpose of the present invention is to provide a method of producing a library including two or more cyclic peptides, wherein at least one of the cyclic peptides included in the library has a structure composed of 4 to 30 amino acids or derivatives thereof and contains, in the structure, at least one selected from cyclic ?-, ?-, and ?-amino acids (cAAs), including a step of preparing an mRNA library encoding a peptide having a sequence represented by the formula (1); —(Xaa)n1- [in the formula (1), Xaas are each an arbitrary amino acid or derivative thereof, at least one Xaa is one selected from cyclic ?-, ?-, and ?-amino acids (cAAs) and n1 is an integer of 2 to 28] and a step of using the mRNA library to express the peptide in a cell-free translation system and produce a library.

Abstract: 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)m-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 R1 and B1 are as defined above, and R3 represents 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).

Abstract: The purpose of the present invention is to provide a method of producing a peptide library including a step of bringing a peptide library including peptides having an amino acid sequence containing at least one Trp or derivative thereof into contact with a prenylation enzyme and prenylating at least a part of amino acid residues contained in at least some of the peptides.

Abstract: The purpose of the present invention is to provide a cyclic peptide having any unit structure selected from the structures represented by the following formula (1): —X1—X2—X3—X4—X5—??(1) (in the formula (1), X1 is I, V or L, or an N-alkylamino acid thereof, X2 is S or T, or an N-alkylamino acid thereof, X3 is K or an N-alkylamino acid thereof, X4 is W or an N-alkylamino acid thereof, and X5 is W, Y, or H, or K or an N-alkylamino acid thereof), or a pharmaceutically acceptable salt of the cyclic peptide.

Abstract: The purpose of the present invention is to provide an efficient and versatile method for granting an additional binding activity to an antibody by inserting a peptide sequence into the antibody. The present invention provides a method of granting a binding ability to a second target molecule to an antibody, comprising inserting an internal peptide sequence of a cyclic peptide into an Fc region of the antibody, wherein the cyclic peptide has the binding ability to the second target molecule different from a first target molecule to be recognized by the antibody.

Abstract: The present invention is directed to a cyclic polypeptide having ubiquitin binding affinity (KD) 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.

Abstract: The present invention provides a sodium taurocholate cotransporting polypeptide (NTCP) inhibitor comprising a cyclic peptide having a Xw1-W-Xw2-W structure, wherein Xw1 and Xw2 are each independently T, S, I, L, or V, or a N-alkylamino acid thereof, or having a P-Xp1-Xp2-H structure, wherein Xp1 is any amino acid, and Xp2 is I, L, or V, or a N-alkylamino acid thereof, or a pharmaceutically acceptable salt thereof.

Abstract: 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.

Abstract: The present invention provides a method of presenting a cyclic peptide on a protein having a loop structure. The cyclic peptide has a chemically crosslinked structure for forming an intramolecular cyclic structure. The method includes replacing the chemically crosslinked structure of the cyclic peptide with two amino acid residues constituting the loop structure, thereby fusing the cyclic peptide with the protein having a loop structure.

Abstract: 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.

Abstract: 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.

Abstract: A material film is formed as a thin film having a thickness of 1 ?m on a surface of a glass substrate. A plurality of micro-chambers having a diameter of 5 ?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.

Abstract: 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 ? 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.

Abstract: 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.

Abstract: 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.