Provided are stapled antimicrobial peptides (i.e., StAMPs) and methods of using the same (e.g., for treating bacterial infections caused by Gram-negative bacteria). In certain embodiments, the stapled peptides are based on the amino acid sequence of the antimicrobial peptide Magainin II, but include certain modifications that have been found to confer advantageous properties (e.g., improved antimicrobial activity, selectivity for killing Gram-negative bacteria, and/or reduced toxicity). Also provided are unstapled peptides which can serve as synthetic precursors to the stapled peptides provided herein

Antimicrobial agents, including antimicrobial peptides (AMPs) and uses thereof. Compositions and methods of using dermaseptin-type and piscidin-type antimicrobial peptides that demonstrate activity and improved therapeutic indices against microbial pathogens, The peptide compositions demonstrate the ability to not only maintain or improve antimicrobial activity against bacterial pathogens including Gram-negative microorganisms Acinetobacter baumannii and Pseudomonas aeruginosa, but also significantly decrease hemolytic activity against human red blood cells. Specificity determinants within the AMPS change selectivity from broad spectrum antimicrobial activity to AMPS with gram-negative selectivity.

An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

The present invention pertains to a novel fusion protein and/or fusion peptide, preferably for use in the separation from and/or detection in an environment of one or more target polymers or plastics, e.g., one or more target polymer fragments and/or particles or target plastic fragments and/or particles, preferably wherein the one or more target polymer particles or target plastic particles are microplastics; a method of preparing such novel fusion protein and/or fusion peptide, a system and kit comprising the novel fusion protein and/or fusion peptide and a (polymer or non-polymer) carrier or carrier system, a use of the novel fusion protein and/or fusion peptide or of a system and kit as mentioned in the separation from and/or detection in an environment of one or more target polymers or plastics, e.g., one or more target polymer fragments and/or particles or target plastic fragments and/or particles, preferably wherein the one or more target polymer particles or target plastic particles are microplastics; a method of separation of one or more target polymers or plastics from an environment, e.g., one or more target polymer fragments and/or particles or target plastic fragments and/or particles, and a method of detection of one or more target polymers or plastics in an environment, e.g., one or more target polymer fragments and/or particles or target plastic fragments and/or particles, preferably wherein the one or more target polymer particles or target plastic particles are microplastics.

The present invention is directed to a cleaning composition including surface active proteins selected from the group consisting of ranaspumins, latherins, and mixtures thereof and a specific surfactant system including one or more anionic surfactants and one or more co-surfactants and wherein the weight ratio of the anionic surfactants to the co-surfactants is less than 9:1. Methods of making and using such compositions are also provided.

Provided are stapled antimicrobial peptides (i.e., StAMPs) and methods of using the same (e.g., for treating bacterial infections caused by Gram-negative bacteria). In certain embodiments, the stapled peptides are based on the amino acid sequence of the antimicrobial peptide Esculentin-1A but include certain modifications that have been found to confer advantageous properties (e.g., improved antimicrobial activity, selectivity for killing Gram-negative bacteria, and/or reduced toxicity). Also provided are unstapled peptides which can serve as synthetic precursors to the stapled peptides provided herein.

Compositions and provided to induce cells of the inner ear to renter the cell cycle and to proliferate. In particular, hair cells are induced to proliferate by administration of a composition which activates the Myc and Notch. Supporting cells are induced to transdifferentiate to hair cells by inhibition of Myc and Notch activity or the activation of Atoh1. Methods of treatment include the intracellular delivery of these molecules to a specific therapeutic target.

The present disclosure provides granzyme-activatable and detectable membrane-interacting peptides that, following activation, can interact with phospholipid bilayers, such as cell membranes. The present disclosure also provides methods of use of such peptides, as well as compositions comprising such peptides. The peptides of the present disclosure are of the general structure X.sup.1a-A-X.sup.2ZX.sup.1b, where A is a membrane-interacting peptide region having a plurality of nonpolar hydrophobic amino acid residues that, following separation from portions Z, is capable of interaction with a phospholipid bilayer; Z is an inhibitory peptide region that can inhibit the activity of portion A; X.sup.2 is a granzyme-cleavable linker that can be cleaved to release cleavage products from the compound; and X.sup.1a and X.sup.1b are optionally-present chemical handles that facilitate conjugation of various cargo moieties to the compound.

Antimicrobial fusion peptides include a polypeptide having at least 35 amino acids and containing the amino acid sequence GIGGALLSAG X.sup.1SALX.sup.2GLAX.sup.3G LAEHFAN, where X.sup.1, X.sup.2, and X.sup.3 independently represent lysine, glutamic acid, or glutamine, and wherein at least one of X.sup.1, X.sup.2, or X.sup.3 is independently selected from glutamic acid or glutamine, including variants with at least 97% sequence homology. Pharmaceutical compositions may include the polypeptides and may be used for treatment of bacterial infection caused by C. acnes. The polypeptides are nonhemolytic and exhibit reduced in vitro cytotoxicity relative to other antimicrobial peptides, which makes them useful in pharmaceutical, healthcare, medical device, food, and personal care applications.

Antimicrobial agents, including antimicrobial peptides (AMPs) and uses thereof. Compositions and methods of using dermaseptin-type and piscidin-type antimicrobial peptides that demonstrate activity and improved therapeutic indices against microbial pathogens. The peptide compositions demonstrate the ability to not only maintain or improve antimicrobial activity against bacterial pathogens including Gram-negative microorganisms Acinetobacter baumannii and Pseudomonas aeruginosa, but also significantly decrease hemolytic activity against human red blood cells. Specificity determinants within the AMPS change selectivity from broad spectrum antimicrobial activity to AMPS with gram-negative selectivity.