Abstract: The present invention relates to the recombinant production of amphiphilic peptides with biologically and therapeutically significant activities. In one embodiment, this invention relates to recombinantly producing an amphiphilic peptide by providing a protease-deficient microbial host transformed with an expression vector containing DNA that encodes the amphiphilic peptide under the control of a regulatory sequence operable in the microbial host and expressing the amphiphilic peptide in the transformed microbial host. In another embodiment, this invention relates to providing an E. coli protease-deficient K-12 cell transformed with a vector that expresses a cleavable fusion protein comprising at least part of a carbohydrate binding protein and the amphiphilic peptide in the cell, expressing the fusion protein in the cell, and cleaving the fusion protein to obtain the amphiphilic peptide substantially free of carbohydrate binding protein residues.

Abstract: The present invention relates to several types of antimicrobial peptides including reverse antimicrobial peptides, antimicrobial oligopeptides and other antimicrobial compositions, such as cecropin P1. The present invention also relates to the use of these antimicrobial peptides to provide organisms, and, in particular, plants, with protection from microbial pathogens. Finally, the present invention relates to a screening method which may be useful for determining the phytotoxity of an antimicrobial peptide.

Abstract: Biologically active amphiphilic peptides including one of the following basic structures: I. R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.1 --R.sub.1 ; II. R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 ; III. R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.3 ; IV. R.sub.1 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.4 ; V. R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.3 ; or VI. R.sub.1 --R.sub. 1 --R.sub.3 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1.R.sub.1 is a hydrophobic amino acid and R.sub.

Abstract: The present invention relates to a number of peptides which have antimicrobial activity and which are useful in retarding plant pathogens. In addition, compounds in accordance with the present invention may have improved resistance to degradation by plant proteases, and/or sufficiently low phytotoxicity to render them likely candidates for use in conjunction with plants. The present invention also relates to oligonucleotides which are capable of expressing the aforementioned peptides. Also provided hereby is a process of retarding the growth of plant pathogens using the compounds of the present invention as well as a screening method and screening reagent useful in determining the proteolytic degradation resistance of a known compound.

Abstract: This invention relates to processes for the microbial production of peptide oligomers, to polypeptide products resulting from application of any of these processes, and to microbes for use in such production. Another aspect of this invention relates to processes for genetically engineering such microbes and to plasmid vectors for use in such engineering.

Abstract: A process for preparing a co-poly(amide/peptide) by reacting polymeric or oligomeric polypeptides and polymeric or oligomeric polyamides in the presence of an effective amount of one or more aryl phosphoryl azide compounds.

Abstract: This invention relates to a process for blow molding polyamide compositions where the molten polyamide includes an effective amount of one or more aryl phosphoryl azide compounds.

Abstract: A diagnostic reagent is disclosed containing a complex of a probe polynucleotide (P) bound via purine/pyrimidine hydrogen bonding to a labeled polynucleotide (L). The probe (P) contains a target binding region (TBR) capable of binding to a target nucleotide sequence (G) of a biological sample. A method is disclosed in which contact with a sample containing the target nucleotide sequence (G) causes binding, initially between G and a single-stranded portion (IBR) of the target binding region (TBR). Thereafter the labeled polynucleotide (L) is displaced from the complex by branch migration of (G) into the (P)/(L) binding region. A volume excluding polymeric agent such as poly(ethylene oxide) (PEO or PEG) or other polyethers enhances the rate of appearance of displaced labeled polynucleotide. Determination of displaced labeled polynucleotide (L) gives a value which is a function of the presence and concentration of target nucleotide sequence (G) in the sample.

Abstract: A diagnostic reagent is disclosed containing a complex of a probe polynucleotide (P) bound via purine/pyrimidine hydrogen bonding to a labeled polynucleotide (L). The probe (P) contains a target binding region (TBR) capable of binding to a target nucleotide sequence (G) of a biological sample. A method is disclosed in which contact with a sample containing the target nucleotide sequence (G) causes binding, initially between G and a single-stranded portion (IBR) of the target binding region (TBR). Thereafter the labeled polynucleotide (L) is displaced from the complex by branch migration of (G) into the (P)/(L) binding region. Determination of displaced labeled polynucleotide (L) gives a value which is a function of the presence and concentration of target nucleotide sequence (G) in the sample.

Abstract: A target nucleotide sequence having a half-restriction site is determined in the nucleic acid of a biological sample. It is contacted with a reagent complex of:(i) a labeled probe polynucleotide containing a target binding region which is substantially complementary to the target nucleotide sequence and which contains a unique half-restriction site completely complementary to the half-restriction site of the target nucleotide sequence; and(ii) a second polynucleotide hybridized to the labeled probe polynucleotide in at least a portion of the target binding region, the portion including the unique half-restriction site of the target binding region;The second polynucleotide contains at least one mismatched or unpaired nucleotide opposite to the unique half-restriction site of the labeled probe polynucleotide, whereby a restriction enzyme specific for the unique restriction site will not cleave the reagent complex.