Patent classifications
C12Y203/01097
Genetically encoded lipid-polypeptide hybrid biomaterials that exhibit temperature triggered hierarchical self-assembly
Disclosed herein are conjugates including a fatty acid, a self-assembly domain, and a polypeptide, where the conjugates have phase transition behavior. Further disclosed are methods of using the conjugates to treat disease, methods of delivering an agent, and methods of preparing the conjugates.
NON-CANONICAL LIPOPROTEINS WITH PROGRAMMABLE ASSEMBLY AND ARCHITECTURE
Artificial lipoproteins bearing non-canonical post-translational modifications that are synthesized by leveraging substrate promiscuity of an acyltransferase. The non-canonical functionality of these lipoprotein results in a distinctive hysteretic assembly that is absent from the canonical lipoproteins and is used to prepare hybrid multiblock materials with precise and programmable patterns of amphiphilicity due to the unique assembly and function of the non-canonical post-translational modifications.
In vivo protein N-acylation
Described are a genetically modified microorganism and corresponding methods and products. The genetically modified microorganism may include a first gene that encodes an acyl transferase and a second gene that encodes a peptide or protein. One or both of the first and second gene may be heterologous. The genetically modified microorganism may include a modified acyl-CoA biosynthetic pathway configured for one or more of: inducible biosynthesis of an acyl-CoA and over-accumulation of the acyl-CoA. The genetically modified microorganism may be effective upon fermentation to cause acylation of the peptide or protein by the acyl transferase using the acyl-CoA to provide a N-acylated peptide or protein product.
In vivo protein N-acylation
Described are a genetically modified microorganism and corresponding methods and products. The genetically modified microorganism may include a first gene that encodes an acyl transferase and a second gene that encodes a peptide or protein. One or both of the first and second gene may be heterologous. The genetically modified microorganism may include a modified acyl-CoA biosynthetic pathway configured for one or more of: inducible biosynthesis of an acyl-CoA and over-accumulation of the acyl-CoA. The genetically modified microorganism may be effective upon fermentation to cause acylation of the peptide or protein by the acyl transferase using the acyl-CoA to provide a N-acylated peptide or protein product.
IN VIVO PROTEIN N-ACYLATION
Described are a genetically modified microorganism and corresponding methods and products. The genetically modified microorganism may include a first gene that encodes an acyl transferase and a second gene that encodes a peptide or protein. One or both of the first and second gene may be heterologous. The genetically modified microorganism may include a modified acyl-CoA biosynthetic pathway configured for one or more of: inducible biosynthesis of an acyl-CoA and over-accumulation of the acyl-CoA. The genetically modified microorganism may be effective upon fermentation to cause acylation of the peptide or protein by the acyl transferase using the acyl-CoA to provide a N-acylated peptide or protein product.
METHOD FOR KNOCKING OUT N-MYRISTOYLTRANSFERASE (NMT) GENE FROM EIMERIA TENELLA
The present disclosure provides a method for knocking out an N-myristoyltransferase (NMT) gene from Eimeria tenella, and belongs to the technical field of microorganisms. The method includes: mixing sporozoites of Eimeria tenella with a pCRISPR::EtNMT plasmid and a pEtNMT::DHFR plasmid, and subjecting a resulting mixture to electrotransformation to obtain NMT gene-knockout Eimeria tenella. The method provided by the present disclosure can successfully knock out the NMT gene from Eimeria tenella, which lays a foundation for studying the function of the Eimeria tenella gene and developing a vaccine therefor.
IN VIVO PROTEIN N-ACYLATION
Described are a genetically modified microorganism and corresponding methods and products. The genetically modified microorganism may include a first gene that encodes an acyl transferase and a second gene that encodes a peptide or protein. One or both of the first and second gene may be heterologous. The genetically modified microorganism may include a modified acyl-CoA biosynthetic pathway configured for one or more of: inducible biosynthesis of an acyl-CoA and over-accumulation of the acyl-CoA. The genetically modified microorganism may be effective upon fermentation to cause acylation of the peptide or protein by the acyl transferase using the acyl-CoA to provide aN-acylated peptide or protein product.
Non-canonical lipoproteins with programmable assembly and architecture and method of making non-canonical lipoproteins
Artificial lipoproteins bearing non-canonical post-translational modifications that are synthesized by leveraging substrate promiscuity of an acyltransferase. The non-canonical functionality of these lipoprotein results in a distinctive hysteretic assembly that is absent from the canonical lipoproteins and is used to prepare hybrid multiblock materials with precise and programmable patterns of amphiphilicity due to the unique assembly and function of the non-canonical post-translational modifications.
GENETICALLY ENCODED LIPID-POLYPEPTIDE HYBRID BIOMATERIALS THAT EXHIBIT TEMPERATURE TRIGGERED HIERARCHICAL SELF-ASSEMBLY
Disclosed herein are conjugates including a fatty acid, a self-assembly domain, and a polypeptide, where the conjugates have phase transition behavior. Further disclosed are methods of using the conjugates to treat disease, methods of delivering an agent, and methods of preparing the conjugates.
NON-CANONICAL LIPOPROTEINS WITH PROGRAMMABLE ASSEMBLY AND ARCHITECTURE
Artificial lipoproteins bearing non-canonical post-translational modifications that are synthesized by leveraging substrate promiscuity of an acyltransferase. The non-canonical functionality of these lipoprotein results in a distinctive hysteretic assembly that is absent from the canonical lipoproteins and is used to prepare hybrid multiblock materials with precise and programmable patterns of amphiphilicity due to the unique assembly and function of the non-canonical post-translational modifications.