Peptides that form adhesive bonds, even in aqueous and/or saline environments, are disclosed. When aggregated, the peptides may be used in methods for producing hydrogels and/or adhesive materials. Synthetic peptide analogs are provided that are designed based on protein sequences found in barnacle adhesive, and may optionally be augmented with chemistry from other organisms that secrete proteins that adhere to substrates. The peptides may be used, for example, in biomedical and aqueous applications. Methods of using the aggregated peptides as adhesives are also provided.

Aspergillus flavus is an opportunistic, saprophytic fungus that infects maize and other fatty acid-rich food and feed crops and produces toxic and carcinogenic secondary metabolites known as aflatoxins. In vitro studies showed a five-fold increase in antifungal activity of AGM182 (vs. tachyplesin1) against A. flavus. Transgenic maize plants expressing AGM182 under maize Ubiquitin-1 promoter were produced through Agrobacterium-mediated transformation. PCR products confirmed integration of the AGM182 gene, while RT-PCR of maize RNA confirmed the presence of AGM182 transcripts. Maize kernel screening assay using a highly aflatoxigenic A. flavus strain (AF70) showed up to 72% reduction in fungal growth in the transgenic AGM182 seeds compared to isogenic negative control seeds.

Compositions and methods are directed to engineered extracellular matrix protein—mussel foot protein fusions for use as a bioadhesive for repairing tissues. The compositions have one or more of: (i) at least one hydrophobic region; (ii) at least one crosslinking region; (iii) at least one tyrosine residue accessible to be enzymatically modified to a DOPA or TOPA side chain; (iv) at least one mussel foot protein; (v) at least one mussel foot protein loop; (vi) at least one human extracellular protein loop; or (vii) at least one of the following sequences: SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6. The elastin-like polypeptide includes at least one non-naturally occurring amino acid or sequence alteration.

The present disclosure discloses an antimicrobial peptide Scyreprocin of Scylla paramamosain and a method thereof, wherein an amino acid sequence of the antimicrobial peptide Scyreprocin comprises a sequence shown in SEQ ID NO 01, and the antimicrobial peptide is expressed and purified by using genetic engineering technology. The recombinant antimicrobial peptide Scyreprocin has advantages of wide antimicrobial spectrum, good antimicrobial effect, and rapid germicidal rate, shows great application significance, and has good application in preparation of antimicrobial agents. The recombinant antimicrobial peptide Scyreprocin has no cytotoxicity to mouse hepatocytes AML12, human liver cells L02, and can be safely used for medical treatment or can be used as a feed composition.

Provided herein are compositions and methods for the assembly of a bioluminescent complex from two or more non-luminescent (e.g., substantially non-luminescent) peptide and/or polypeptide units. In particular, bioluminescent activity is conferred upon a non-luminescent polypeptide via structural complementation with another, complementary non-luminescent peptide.

Peptides that form adhesive bonds, even in aqueous and/or saline environments, are disclosed. When aggregated, the peptides may be used in methods for producing hydrogels and/or adhesive materials. Synthetic peptide analogs are provided that are designed based on protein sequences found in barnacle adhesive, and may optionally be augmented with chemistry from other organisms that secrete proteins that adhere to substrates. The peptides may be used, for example, in biomedical and aqueous applications. Methods of using the aggregated peptides as adhesives are also provided.

Antimicrobial peptides of general formula X.sub.0X.sub.1X.sub.2CX.sub.3X.sub.4X.sub.5CX.sub.6X.sub.7X.sub.8X.sub.9CYX.sub.10X.sub.11CX.sub.12X.sub.13 are provided. Also provided are certain formulations containing these peptides and methods of using these peptides for treating skin infections in an animal in need thereof.

The disclosure provides a method of generating a sterile fish, crustacean, or mollusk. The method comprises breeding (i) a fertile hemizygous mutated female fish, crustacean, or mollusk with (ii) a fertile hemizygous mutated male fish, crustacean, or mollusk, selecting a female progenitor that is homozygous by genotypic selection, and breeding the homozygous female progenitor to produce the sterile fish, crustacean, or mollusk. The mutation disrupts the maternal-effect of a primordial germ cell (PGC) development gene and does not impair the viability, sex determination, fertility, or a combination thereof, of a homozygous progenitor. The disclosure also provides methods of making broodstock freshwater and seawater organisms for use in producing sterilized freshwater and seawater organisms, as well as the broodstock itself.

The present disclosure describes analog conotoxin peptides of the α-conotoxin peptide RgIA. These analog conotoxin peptides block the α9α10 subtype of the nicotinic acetylcholine receptor (nAChR) and can be used for treating pain and inflammation including inflammatory pain, cancer related pain, and neuropathic pain. The RgIA analogs described in the present invention include a variety of sequence modifications and chemical modifications that are introduced to improve the drug-like characteristics of RgIA analogs and thereby increase their therapeutic value.

An oyster peptide capable of enhancing a sexual function, and a preparation method and application thereof are provided. In the method, oyster meat is pre-treated by using calcium salt before enzymatic hydrolysis, so as to activate and release endogenous enzymes of oysters, such that enzymatic preparations consumed in subsequent enzymatic hydrolysis can be reduced.