4 results about "Random Peptide Library" patented technology

The application discloses a dual-epitope llama-derived nanobody and application thereof, and belongs to the field of biological medicine. The application is aimed at different epitopes of MERS-CoV, and two strains of antibodies 2-77 and 4-58 aiming at different binding sites of MERS-CoV RBD are obtained by immunizing a llama, performing specific screening on a ribosome display nanobody library, performing a pseudovirus neutralization experiment, performing a competitive BLI experiment, identifying VHH epitopes and molecular docking by using a phage random peptide library, and constructing a dual-epitope llama-derived nanobody 2F4 with good neutralization activity, high expression and stability by using the two strains of nanobodies. It is proved by a lesion formation test and a mouse in-vivo experiment that the dual-epitope llama-derived nanobody 2F4 constructed by the application can effectively neutralize MERS-CoV and effectively protect animals, and the application provides a train of thought and technical support for exploring new antigen epitopes of MERS-CoV and designing a therapeutic antibody drug.

The present application relates to the technical field of pest control, in particular to a short peptide simulating a Cry1Ac protein anti-insect function epitope and application thereof. The present application takes a cotton bollworm middle intestine cadherin fragment (HaCad-TBR) as a target, and carries out screening on a phage display random 6-peptide library constructed by the laboratory, to obtain a 6-peptide LTETGK capable of combining with the cotton bollworm middle intestine cadherin, i.e. the 6-peptide has the effect of simulating a key anti-insect function epitope of the Cry1Ac protein, and a recombinant insecticidal protein C8CL2 having good insecticidal activity on the cotton bollworm can be obtained by replacing Loop2 of Domain II in the Cry1Ac. The present application expands the diversity of anti-insect materials of the Cry1Ac protein, and provides a potential alternative new material for preventing and controlling target pests, and can be used for the prevention and control of Lepidoptera pests, and provides technical support for the development of Lepidoptera pest control products.

The application discloses a pathogenic Vibrio Pir B virulence protein binding peptide P2 and application thereof. The small-molecule binding peptide P2 has high affinity with the Pir B virulence protein and has an amino acid sequence of LGSPLLTYGRPQ. The application screens the binding peptide with high affinity with the pathogenic Vibrio Pir B virulence protein from a random peptide library through phage display technology, and the binding peptide is chemically synthesized. After injection of the binding peptide, the survival rate of shrimps after infection with Vibrio can be effectively improved, and the shrimps have a remarkable protection effect in shrimp culture. The binding peptide can efficiently bind to the pathogenic Vibrio Pir B virulence protein, and effectively reduce the virulence of the Pir B protein. In addition, the method can effectively reduce the use of antibiotics in healthy shrimp culture, reduce the generation of drug-resistant strains, and has a good application prospect in the prevention and treatment of shrimp AHPND.

The invention discloses a method for directionally screening a peptide fragment combined with a target protein based on FASP-IP-MS, and belongs to the technical field of biology. The invention aims to identify an interaction proteome of two chitin synthase PsCHS1 and PsCHS2 in phytophthora sojae as target spots, and design an FASP-IP-MS method to determine a method for directionally screening a peptide fragment combined with a target protein on the basis of FASP-IP-MS. The method comprises the following steps: taking the two chitin synthase PsCHS1 and PsCHS2 in phytophthora sojae as target spots, identifying the interaction proteome of the two chitin synthase PsCHS1 and PsCHS2 as target spots, and designing an FASP-IP-MS method. According to the invention, peptide fragments interacting with PsCHS1ECD and PsCHS2ECD in TUB9 are screened based on an ultrafiltration tube assisted proteolysis-in vitro immunoprecipitation-mass spectrometry method. The method has two advantages that on one hand, the random peptide library is obtained through enzymolysis, chemical synthesis is not needed, the cost is lower, and the required time is shorter; and on the other hand, the random peptide library is derived from the known interaction protein, the success rate of screening the interaction peptide fragment is higher, and the method has important significance for improving the level of a peptidomics analysis technology.