63 results about "Proteolytic degradation" patented technology

Compositions and methods for protecting a plant from an insect pest are provided. The invention provides mutagenized nucleic acids that have been engineered to encode pesticidal polypeptides having increased resistance to proteolytic degradation by a plant protease. In particular, nucleic acid sequences encoding pesticidal polypeptides modified to comprise a proteolytic protection site that confers resistance to degradation or proteolytic inactivation by a plant protease are provided. Particular embodiments of the invention provide expression cassettes and transformed plants, plant cells, and seeds. These compositions find use in methods for protecting a plant from a pest.

The present invention relates to novel muteins of human fibroblast growth factor-21 with reduced susceptibility for proteolytic degradation when expressed in yeast. Both protein and the respective encoding nucleic acid species are disclosed. The invention also embodies vectors and host cells for the propagation of said nucleic acid sequences and the production of said muteins. Also disclosed are methods for treating type 2 diabetes, obesity, or metabolic syndrome. X-16816

Novel peptide derivatives, compositions containing them, and their use for treating medical disorders resulting from a deficiency in growth hormone are disclosed. The peptides have the formula (1):wherein a, b, A, R1, L1, D, R3, R4, R2, L2, E and G are as defined in the specification. These peptides exhibit improved resistance to proteolytic degradation, and hence, improved bioavailability.

The disclosed invention relates to methods of modifying peptide compositions to increase stability and delivery efficiency. Specifically, the disclosed invention relates to methods to increase the stability and delivery efficiency of protein kinase C (PKC) modulatory peptide compositions. A “therapeutic peptide composition” comprises a “carrier peptide” and a “cargo peptide.” A “carrier peptide” is a peptide or amino acid sequence within a peptide that facilitates the cellular uptake of the therapeutic peptide composition. The “cargo peptide” is a PKC modulatory peptide. Peptide modifications to either the carrier peptide, the cargo peptide, or both, which are described herein increase the stability and delivery efficiency of therapeutic peptide compositions by reducing disulfide bond exchange, physical stability, reducing proteolytic degradation, and increasing efficiency of cellular uptake.

The invention is directed to the use of (i) a first antigen corresponding to a target antigen of interest, together with (ii) a second antigen, corresponding to a modified form of the target antigen, whose rate of intracellular proteolytic degradation is increased, enhanced or otherwise elevated relative to the first antigen, in compositions and methods for inducing both humoral and cellular immunity in an individual. The ability to provide compositions, which are capable of inducing both host-protective antibody and cell-mediated immune responses, facilitates the generation of immunogenic compositions capable of combating, inter alia, conditions that have long latency periods and, therefore, benefit from the dual approach of prophylaxis and therapy in one delivery.

The identification of the most sensitive sites of Clostridium histolyticum collagenase Class 1 to proteolysis by proteases present during the fermentation and purification of the enzyme is described. Culture supernatant obtained after fermentation of C. histolyticum is used as the starting material for further purification of the enzyme. Native collagenase Class 1 and its proteolytic fragments are partially purified by a combination of hydrophobic interaction and strong anion exchange chromatographies. The pools containing enriched levels of the proteolytic fragments are further purified by high performance anion exchange chromatography. These polypeptides are then characterized by Q-TOF mass spectroscopy. A total of three sensitive bonds are identified along with substitution and deletion strategies that will result in resistance of the enzyme to proteolytic degradation.

Disclosed is an oral delivery system that overcomes major barriers encountered in the gastrointestinal tract, particularly rapid proteolytic degradation and low intestinal permeability. Provided is a method for oral delivery of an engineered microorganism to a mammal where the microorganism produces a macromolecule having a desired bioavailability outcome.

The present invention relates to growth hormone (GH) compounds having additional disulphide bridges and at least one additional single point mutation making the compounds resistant to proteolytic degradation.

Prosthetic compounds are disclosed that are effective for radiolabeling biomolecules with 18F. Representative biomolecules include antibodies (e.g., monoclonal antibodies (mAbs) and nanobodies (sdAbs)), antibody fragments, and peptides that may have an affinity for particular types of cells, such as cancer cells. The prosthetic compounds effectively address the art-recognized difficulties associated with the retention of radioactivity within the targeted cells, due to internalization of the biomolecule, followed by proteolytic degradation. Representative prosthetic compounds include (i) a succinimidyloxycarbonyl moiety, (ii) a radioactive moiety bearing 18F, and (iii) a charged moiety, i.e., a moiety that is charged under the physiological conditions of the internal cell environment.

Retro-inverso peptides derived from interleukin-6 (IL-6) having between 17 and about 40 amino acids and including the sequence shown in SEQ ID NO: 1. These peptides have the same activity as native IL-6 and also have neurotrophic activity. Because of the D-amino acid linkage in the peptides, they are less susceptible to proteolytic degradation in vivo.

Soluble, self-assembling collagens derived from tissues are extensively characterized such that one can predict and customize the final collagen-fibril matrix with respect to fibril microstructure (i.e., fibril density, interfibril branching), viscoelasticity and proteolytic degradability. As shown herein these matrices template and direct the deposition of mesoporous silica at the level of individual collagen fibrils. The fibril density, silicic acid concentration, and time of exposure to silicifying solution were varied and the resulting hybrid materials were analyzed by scanning electron microscopy, energy-dispersive x-ray spectroscopy, and rheology. Microstructural properties of the collagen-fibril template are preserved in the silica surface of hybrid materials. Results for three different collagen fibril densities, corresponding to shear storage moduli of 200 Pa, 1000 Pa, and 1600 Pa, indicate that increased fibril density increases the absolute amount of templated silica when all other silica synthesis conditions are kept constant. The mechanical properties of the hybrid material are dominated by the presence of the silica coating rather than the starting collagen matrix stiffness.