7 results about "Helical peptide" patented technology

The present invention provides an antigen-binding protein comprising a knob domain or a portion thereof capable of binding to an antigen wherein the knob domain or the antigen-binding portion thereof is fused at its N-or C-terminus or both ends directly or via a linker to a helical peptide, preferably an alpha-helical peptide. The invention also relates to the production and use of such antigen binding proteins. The invention further relates to antigen binding proteins for use in therapy.

In various embodiments alpha helical peptide-based bridges for molecular biosensing “on-chip” are disclosed. The Peptide-based bridges serve as common bridges for great diversity of biosensing applications and targets including nucleic acids, proteins, antigens, antibodies, small molecules. The primary sensor element is preferably a “molecular wire” such as an alpha-helical peptide integrated into a current monitoring circuit. The engineered peptide may contain a central conjugation site for attachment of various probe molecules including nucleic acids, proteins, antigens, antibodies. The probe-containing bridge empowers the sensor to detect interactions with specific target molecules.

The present application relates to the field of biotechnology, in particular to a pair of mutually recognizing and combining alpha helix peptides and application thereof. The alpha helix peptide 1 has an amino acid sequence as shown in SEQ ID No. 1, and the alpha helix peptide 2 has an amino acid sequence as shown in SEQ ID No. 2. The cells are combined with each other by a pair of mutually recognizing and combining alpha helix peptides, so that the cells are arranged in a desired manner. The suitable material concentration and action time are verified; the formed cell group morphology is observed by various microscopes; two kinds of models are successfully constructed; and the improvement of cell function by adding DPH material is verified.

A protein-based probe for detecting the presence of one of two distinct states of a target membrane-associated molecule by means of polarization microscopy is disclosed. The probe contains an anchoring moiety consisting of at least one lipidated peptide and / or at least one transmembrane α-helical peptide, a peptide linker moiety having the length of at least 5 amino acids, wherein at least 50% of the amino acids forming the linker are selected from glycine, serine, and threonine, a fluorescent moiety, and an affinity binding moiety capable of binding the target membrane-associated molecule. The moieties are arranged in the order a-b-c-d or d-c-b-a in the direction from the N-terminus to the C-terminus. Methods of detecting presence or absence of the target molecule, detecting activated or inactive forms of the target molecule, and detecting the activation of the target molecule are also described.

The present invention relates to a fusion polypeptide and a method for purifying a target protein by using same, the polypeptide having any one from among a His tag, a HAT tag and an HQ tag, and an α-helix peptide tag of which the major amino acids are charged and hydrophobic amino acids. Since the fusion polypeptide has an ability to induce self-assembly by being fused with the target protein, the target protein purification method using same enables the isolation and purification of the target protein merely through very simple processes such as centrifugation or filtration.

The invention provides a broad-spectrum antibacterial peptide KVL4 as well as a preparation method and application thereof, and belongs to the technical field of biology, and the amino acid sequence of the broad-spectrum antibacterial peptide KVL4 is shown as SEQ ID No.1. Design is carried out on the basis of an alpha-helical peptide template (abcdefg) n, n = 4, positions a, d and f are hydrophobic amino acids, and Val, Leu and Trp are adopted in sequence; positive charge amino acid Lys is adopted at positions b, c and e; and negative charge amino acid Glu is adopted at the position g to promote spiral association. The antibacterial peptide KVL4 has an inhibition effect on various bacteria such as escherichia coli, salmonella typhimurium and staphylococcus aureus, and the average antibacterial activity is as low as 5.84 mu M. And the high-concentration KVL4 shows good biocompatibility on both human red blood cells and porcine jejunum epithelial cells IPEC-J2. In conclusion, the antibacterial peptide KVL4 is an antibacterial peptide with relatively high application potential.

The invention provides structurally-constrained peptides by hydrocarbon stapling of a BCL9 HD2 helix for use as a therapeutic agent. The invention further provides methods and kits for use of the structurally-constrained peptide of the instant invention. The invention is based, at least in part, on the results provided herein demonstrating that hydrocarbon stapled helical peptides display excellent proteolytic, acid, and thermal stability, restore the native helical structure of the peptide, possess superior pharmacokinetic properties compared to the corresponding unmodified peptides, and are highly effective in binding to β-catenin in vitro, in cellulo, and in vivo, disrupting the BCL9 / β-catenin interaction, and thereby interfering with deregulated Wnt / β-catenin signaling for therapeutic benefit in a variety of human diseases including human cancer.