A composition comprising as components a polypeptide IMPI (including wild type) and/or a polypeptide IMPI-fusion and at least one antibiotic compound, in particular an aminoglycoside antibiotic, and/or at least one bactericidal compound, wherein the polypeptides, the at least one antibiotic and the at least one bactericidal compound is present in the composition in concentrations which exhibit in combination a synergistic effect against resistant bacteria.

Polypeptides or proteins comprising tissue inhibitor of mettaloproteinases-3 (TIMP3) or variants of TIMP3 can be used to substantially inhibit vascular endothelial growth factor (VEGF) binding to VEGF receptor-2 (VEGFR2/KDR/Flk-1)) without substantially inhibiting VEGF binding to VEGF receptor 1 (VEGFR1/Flt-1).

The invention relates to a method for inhibiting an ADAM protease, comprising inhibiting binding to an integrin-binding loop of a disintegrin domain in the ADAM protease. Also provided are cyclic peptides which inhibit binding to an integrin-binding loop of an ADAM protease, as well as associated pharmaceutical compositions, uses and methods of treatment.

Disclosed herein is a method of reprogramming highly motile cells found in tumors, such as these highly motile GSC and/or MDSC clones, into auto-destructive cell missiles (referred to herein as therapeutic stealth cells) that can seek and destroy new foci of recurrence within the body, such as the brain. Cells with enhanced motility can be sorted out from heterogeneous populations and then be rendered auto-destructive by deterministic delivery of an anti-cancer agent, such as an oncolytic virus plasmid cocktail.

MMP-8 activation products are disclosed that have a MMP-8 middle-part activation product having a size between 20-35 kDa. Methods of detecting the MMP-8 activation product or activated MMP-8 fragments in a biological sample derived from a subject are also disclosed. The MMP-8 activation product or activated MMP-8 fragments diagnose diseases based on abnormal or elevated levels of activated MMP-8.

The invention relates to a method for inhibiting an ADAM protease, comprising inhibiting binding to an integrin-binding loop of a disintegrin domain in the ADAM protease. Also provided are cyclic peptides which inhibit binding to an integrin-binding loop of an ADAM protease, as well as associated pharmaceutical compositions, uses and methods of treatment.

A novel composition and method of enhancing wound healing and minimizing rejection of an implant is presented. The composition is a dry acellular mixture comprised of conditioned media from mesenchymal stem cells, a multifunctional protease inhibitor, and a tethering peptide that acts as a tether to keep the composition in contact with the targeted area. An antimicrobial fusion peptide may also be added to the composition.

Disclosed herein is a method of reprogramming highly motile cells found in tumors, such as these highly motile GSC and/or MDSC clones, into auto-destructive cell missiles (referred to herein as therapeutic stealth cells) that can seek and destroy new foci of recurrence within the body, such as the brain. Cells with enhanced motility can be sorted out from heterogeneous populations and then be rendered auto-destructive by deterministic delivery of an anti-cancer agent, such as an oncolytic virus plasmid cocktail.

The present disclosure discloses use of a fused polypeptide with multifunctional activities. In the fused polypeptide with multifunctional activities, the polypeptide contains the following domains: Pro-Arg-Cys-X-Y-Gly-Glu, where X is Trp or Tyr, and Y is Arg or Cys; and Gly-Gly-Gly-Gly-Ile-Val-Arg-Arg-Ala-Asp-Arg-Ala-Ala-Val-Pro-Gly-Gly-Gly-Gly-Arg-Gly-Asp; or a sequence of any amino acid mutated in the foregoing domains. The fused polypeptide can be used for treating various fibrosis diseases and symptoms, including pulmonary fibrosis, hepatic fibrosis, skin fibrosis, renal fibrosis, myocardial fibrosis, and lung tissue lesions.

A modified Ac-TMP-2 protein lacks one or a plurality of acidic C-terminal amino acids normally present in a full-length or wild-type Ac-TMP-2 protein and may also lack one or a plurality of N-terminal amino acids while retaining the amino acid sequence CSC at or near the N-terminus. The modified Ac-TMP-2 protein may be useful in method and composition for reducing or alleviating inflammation in a subject. Inflammation may be associated with a disease is a disease of the digestive tract such as chronic gastritis or an inflammatory bowel disease such as Crohn's disease or ulcerative colitis, or a disease of the respiratory system, such as asthma, emphysema, chronic bronchitis, and chronic obstructive pulmonary disease.