The present invention relates to a receptor-binding domain of an IgE-dependent histamine releasing factor (HRF), and a use thereof, and more specifically, ascertains, as an HRF structural region, and a FL domain and an H2 domain which bind to a receptor of HRF existing in a cell membrane, ascertains the C-terminus domain of the HRF, and ascertains that a material binding thereto inhibits IL-8 secretion, thereby determining that the FL and H2 domains and the C-terminus domain can be utilized in: the development of a therapeutic agent for treatment and prevention of HRF-related disease including allergic diseases such as asthma, rhinitis, atopic dermatitis, and anaphylaxis; inflammatory diseases such as rheumatoid arthritis; and malaria, and a method for screening for the HRF-related diseases.

The present invention relates to a receptor-binding domain of an IgE-dependent histamine releasing factor (HRF), and a use thereof, and more specifically, ascertains, as an HRF structural region, and a FL domain and an H2 domain which bind to a receptor of HRF existing in a cell membrane, ascertains the C-terminus domain of the HRF, and ascertains that a material binding thereto inhibits IL-8 secretion, thereby determining that the FL and H2 domains and the C-terminus domain can be utilized in: the development of a therapeutic agent for treatment and prevention of HRF-related disease including allergic diseases such as asthma, rhinitis, atopic dermatitis, and anaphylaxis; inflammatory diseases such as rheumatoid arthritis; and malaria, and a method for screening for the HRF-related diseases.

Disclosed herein are synthetic hydrogels suitable for delivering antimicrobial proteins, optionally in combination with bone regenerating agents to injured tissues. The hydrogels can include lysostaphin and one or more bone morphogenic proteins. The hydrogels are composed of a network of crosslinked hydrophilic polymers and adhesion peptides.

Disclosed herein are synthetic hydrogels suitable for delivering antimicrobial proteins, optionally in combination with bone regenerating agents to injured tissues. The hydrogels can include lysostaphin and one or more bone morphogenic proteins. The hydrogels are composed of a network of crosslinked hydrophilic polymers and adhesion peptides.

Provided is a method for treating cancers expressing immune checkpoint protein PD-L1. Also provided is a method for reducing PD-L1 expression of cancer cells by administering to a subject in need thereof an effective amount of an immunomodulatory protein of Ganoderma, a recombinant thereof, or a fungal immunomodulatory protein of a similar structure.

Provided is a method for treating cancers expressing immune checkpoint protein PD-L1. Also provided is a method for reducing PD-L1 expression of cancer cells by administering to a subject in need thereof an effective amount of an immunomodulatory protein of Ganoderma, a recombinant thereof, or a fungal immunomodulatory protein of a similar structure.

The present disclosure pertains to the use of an immunomodulatory protein in preventing, inhibiting and/or reducing coronavirus (CoV) infections. The Ganoderma immunomodulatory protein, a recombinant thereof or a fragment thereof of the disclosure is able to induce ACE2 degradation via activating the protein degradation system.

The present disclosure pertains to the use of an immunomodulatory protein in preventing, inhibiting and/or reducing coronavirus (CoV) infections. The Ganoderma immunomodulatory protein, a recombinant thereof or a fragment thereof of the disclosure is able to induce ACE2 degradation via activating the protein degradation system.

A polypeptide composition for treating atrial fibrillation includes a polypeptide that has a sequence: fADNYTRLRKQMAVKKYLNSILN-NH.sub.2 (SEQ ID NO: 1), ##STR00001##
From an N-terminus of the polypeptide, a first amino acid (f) is a D-Phe, a second amino acid is Ala, and a third amino acid is Asp; and the peptide is linear in a solution and forms an α-helix structure after encountering a lipid bilayer.

A polypeptide composition for treating atrial fibrillation includes a polypeptide that has a sequence: fADNYTRLRKQMAVKKYLNSILN-NH.sub.2 (SEQ ID NO: 1), ##STR00001##
From an N-terminus of the polypeptide, a first amino acid (f) is a D-Phe, a second amino acid is Ala, and a third amino acid is Asp; and the peptide is linear in a solution and forms an α-helix structure after encountering a lipid bilayer.