A pharmaceutical composition for treating Gram negative bacteria-associated infections includes an antibacterial protein that includes at least one selected from the group consisting of a protein having the amino acid sequence as set forth in SEQ ID NO: 1, a protein having the amino acid sequence as set forth in SEQ ID NO: 2, a protein having the amino acid sequence as set forth in SEQ ID NO: 3, a protein having the amino acid sequence as set forth in SEQ ID NO: 4, a protein having the amino acid sequence as set forth in SEQ ID NO: 5, a protein having the amino acid sequence as set forth in SEQ ID NO: 6, a protein having the amino acid sequence as set forth in SEQ ID NO: 7, and a protein having the amino acid sequence as set forth in SEQ ID NO: 8. A method of preparing the antibacterial protein is also disclosed.

The present invention provides a new building block for peptide synthesis, which introduces a cleavage site that can be used to generate cleavable fragments subsequent to a peptide sequence.

A method for searching for a modification site of a peptide molecule includes: calculating, by a computer, a second steric structure of the peptide molecule by using data of a first steric structure of the peptide molecule, the first steric structure being a steric structure of the peptide molecule in a complex structure of a target molecule and the peptide molecule, the second steric structure being a stable steric structure of the peptide molecule in a state where a steric configuration of a main chain of the peptide molecule in the first steric structure is fixe; and comparing data of the second steric structure with the data of the first steric structure in order to search for a side chain having a difference in steric configuration between the two steric structures.

[Problem to be Solved]

To provide a compound for removing pluripotent cells from a cell population potentially containing the pluripotent cells.

[Solution]

A polyphenylalanine derivative is contacted with a cell population of interest.

The present invention relates to a short peptide-based therapeutic agent and a medicinal composition including the same for inhibiting activities of cancer cells, which includes at least one short peptide listed as SEQ ID NOs: 1 and 2, either of which is unglycosylated and has no more than 40 amino acid residues, thereby specifically reducing or inhibiting activities of cancer cells such as the cancer cell proliferation, cancer stemness, cell migration, cancer cell invasion, metastasis or drug resistance.

Disclosed is a stable pharmaceutical solution formulation of a GLP-1R antibody fusion protein, comprising a therapeutically effective amount of the GLP-1R antibody fusion protein, an amino acid, a surfactant and a buffer system. The final concentration of the amino acid is 1-500 mM, the final concentration of the surfactant is 0.01%-0.5%, and the pH value of the stable solution formulation is from 5.0 to 8.0. The stable solution formulation of the present invention can be used in the treatment of diabetes, obesity and conditions associated therewith.

Described herein are variants of alpha-hemolysin having at least one amino acid substitution at H35G, E111N, M113A, and/or K147N in the mature, wild-type alpha-hemolysin amino acid sequence. In certain examples, the variant may have a substitution at E111S, M113S, T145S, K147S, or L135I in the mature alpha-hemolysin amino acid sequence. The α-hemolysin variants may also include a substitution at H144A and/or a series of glycine residues spanning residues 127 to 131 of the mature, wild-type alpha hemolysin. Also provided are nanopore assemblies including the alpha-hemolysin variants, the assembly having an increased nanopore lifetime. Further, provided are variants that, in addition to providing increased lifetime, provide a decreased time-to-thread. Hence, the variants provided herein both increase nanopore lifetime and improve efficiency and accuracy of DNA sequencing reactions using nanopores comprising the variants.

This invention is related to novel PNA probes, probe sets, methods and kits pertaining to the detection of one or more species of Candida yeast. Non-limiting examples of probing nucleobase sequences that can be used for the probes of this invention can be selected from the group consisting of: AGA-GAG-CAG-CAT-GCA (Seq. Id. No. 1), AGA-GAG-CAA-CAT-GCA (Seq. Id. No. 2), ACA-GCA-GAA-GCC-GTG (Seq. Id. No. 3), CAT-AAA-TGG-CTA-CCA-GA (Seq. Id. No. 4), CAT-AAA-TGG-CTA-CCC-AG (Seq. Id. No. 5), ACT-TGG-AGT-CGA-TAG (Seq. Id. No. 6), CCA-AGG-CTT-ATA-CTC-GC (Seq. Id. No. 7), CCC-CTG-AAT-CGG-GAT (Seq. Id. No. 8), GAC-GCC-AAA-GAC-GCC (Seq. Id. No. 9), ATC-GTC-AGA-GGC-TAT-AA (Seq. Id. No. 10), TAG-CCA-GAA-GAA-AGG (Seq. Id. No. 11), CAT-AAA-TGG-CTA-GCC-AG (Seq. Id. No. 12), CTC-CGA-TGT-GAC-TGC-G (Seq. Id. No. 13), TCC-CAG-ACT-GCT-CGG (Seq. Id. No. 14), TCC-AAG-AGG-TCG-AGA (Seq. Id. No. 15), GCC-AAG-CCA-CAA-GGA (Seq. Id. No. 16), GCC-GCC-AAG-CCA-CA (Seq. Id. No. 17), GGA-CTT-GGG-GTT-AG (Seq. Id. No. 18), CCG-GGT-GCA-TTC-CA (Seq. Id. No. 19), ATG-TAG-AAC-GGA-ACT-A (Seq. Id. No. 20), GAT-TCT-CGG-CCC-CAT-G (Seq. Id. No. 21), CTG-GTT-CGC-CAA-AAA-G (Seq. Id. No. 22) and AGT-ACG-CAT-CAG-AAA (Seq. Id. No. 23).

The present invention relates, inter alia, to ghrelin analogues and their medical use, for example in the treatment of cachexia, chronic obstructive pulmonary disease, gastrointestinal disorders (e.g., gastroparesis and/or inflammatory disorders such as colitis, gut barrier dysfunction, and ischemia reperfusion injury), loss of body weight, and decreased appetite.

Non-natural albumin binding domains, polynucleotides encoding thereof and methods of making and using these domains and polynucleotides are useful in controlling the half-life of therapeutic molecules for patients.