Patent classifications
C40B40/10
DESIGN AND SELECTION OF AFFINITY AGENTS
Methods and systems are provided herein for selecting an affinity reagent which binds a desired peptide epitope in a plurality of sequence contexts. The method relies on obtaining a peptide library, each peptide having the sequence αXβ, wherein X is the desired peptide epitope, wherein each of α and β comprise an amino acid, using the peptide library to select an affinity reagent.
HLA-based methods and compositions and uses thereof
Compositions and methods for isolating HLA-peptides from cells. A universal platform and methods for profiling the HLA-peptidome, enabling identification of endogenously presented HLA-peptides from cell lines expressing any possible class I or II construct.
RIGID HELICAL JUNCTIONS FOR MODULAR REPEAT PROTEIN SCULPTING AND METHODS OF USE
Disclosed herein are junction polypeptides that can be used, for example, to join together protein building blocks via a rigid fusion to generate a wide range of protein shapes; fusion proteins comprising such junction polypeptides, polymers thereof, and methods for designing such junction polypeptides.
A GENETICALLY ENCODED, PHAGE-DISPLAYED CYCLIC PEPTIDE LIBRARY AND METHODS OF MAKING THE SAME
Embodiments of the present disclosure pertain to methods of selecting cyclic peptides that bind to a target by transforming a phage display library with a plurality of nucleic acids into bacterial host cells, where the nucleic acids include phage coat protein genes with a combinatorial region that encodes at least one cysteine and at least one non-canonical amino acid. The transformation results in the production of phage particles with phage coat proteins where the cysteine and the non-canonical amino acid couple to one another to form a cyclic peptide library. Phage particles are then screened against the desired target to select bound cyclic peptides. Amino acid sequences of the selected cyclic peptides are then identified. Additional embodiments pertain to methods of constructing a phage display library that encodes the cyclic peptides. Further embodiments of the present disclosure pertain to the produced cyclic peptides, phage display libraries and phage particles.
Vectors for Producing Virus-Like Particles and Uses Thereof
The present disclosure provides expression vectors and bacterial sequence-free vectors, such as ministring DNA (msDNA), for producing virus-like particles (VLPs) as well as compositions and methods thereof. In some aspects, the methods include treating viral infections in subjects with the vectors, compositions, and VLPs.
SYSTEM AND METHOD OF MODULAR CLONING
System for producing a nucleic acid construct of interest, said system comprising: a set of n entry DNAs numbered 1 to n, n being an integer of at least 2, each of said n entry DNAs comprising in this order: (i) a type IIs restriction endonuclease recognition site followed by the cleavage site thereof; (ii) a sequence portion linking the cleavage site of said recognition site of item (i) with the cleavage site of the recognition site of the following item (iii), and (iii) a cleavage site of a further type IIs restriction endonuclease recognition site followed by the recognition site of said cleavage site; the cleavage sites of the type IIs restriction endonuclease recognition sites of item (iii) of entry DNAs 1 to n−1 are complementary to the cleavage sites of the type IIs restriction endonuclease recognition sites of item (i) of entry DNAs 2 to n, respectively; the cleavage site of the type IIs restriction endonuclease recognition site of item (iii) of entry DNA n is complementary to the cleavage site of the type IIs restriction endonuclease recognition site of item (i) of entry DNA 1 for allowing annealing of complementary single-stranded overhangs formed by restriction at recognition site (i) of entry DNA 1 and at recognition site (iii) of entry DNA n; said system further comprising a destination vector comprising in this order: (I) a type IIs restriction endonuclease recognition site followed by the cleavage site thereof; (II) a vector backbone preferably comprising a selectable marker gene, said vector backbone linking the cleavage sites of said recognition sites of items (I) and the following item (III); (III) a further cleavage site of a type IIs restriction endonuclease recognition site followed by the recognition site of said cleavage site, and (IV) optionally, an insert between the recognition sites of item (III) and item (I); said cleavage sites of items (I) and (III) being different and non-complementary, said recognition sites of items (I) and (III) being preferably recognitions sites of the same endonuclease.
METHOD FOR PREPARING NOVEL ANTIBODY LIBRARY AND LIBRARY PREPARED THEREBY
The present invention relates to a method for preparing a novel antibody library and a library prepared thereby. The antibody library prepared according to the present invention contains antibodies having excellent physical properties against a plurality of antigens, thereby having functional diversity and containing a plurality of unique sequences, and thus can be favorably used as an antibody library.
Recombinant polyclonal proteins targeting COVID-19 and methods of use thereof
Provided herein are compositions comprising recombinant polyclonal proteins (RPPs) derived from mammalian plasma cells and plasmablasts. Also provided are methods of using the RPPs.
Recombinant polyclonal proteins targeting COVID-19 and methods of use thereof
Provided herein are compositions comprising recombinant polyclonal proteins (RPPs) derived from mammalian plasma cells and plasmablasts. Also provided are methods of using the RPPs.
STABILIZED FIBRONECTIN BASED SCAFFOLD MOLECULES
Provided herein are proteins comprising a fibronectin based scaffold (FBS) domain, e.g., .sup.10Fn3 molecules, that bind specifically to a target, and wherein the FBS domain is linked at its C-terminus to a region consisting of PmXn, wherein P is proline, X is any amino acid and wherein n is 0 or an integer that is at least 1 and m is an integer that is at least 1, and wherein the PmXn moiety provides an enhanced property to the FBS domain, e.g., enhanced stability, relative to the protein that is not linked to the PmXn moiety.