13 results about "Helical peptide" patented technology

Provided are: lipid-containing nanoparticles that replace a reconstituted high-density lipoprotein (rHDL); and a composition comprising said lipid-containing nanoparticles. This complex comprises a complex lipid and an apolipoprotein A-I-derived helix 4 (H4) peptide, wherein the H4 peptide has an amino acid sequence of YLDDFQKKWQEEMELYRQKVE (SEQ NO. 1) and has a C-terminus that may be amidated. This composition comprises a complex according to the present invention. The composition can be for cosmetic use or percutaneous absorption drug use, or for the treatment of inflammatory diseases.

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.

Compositions and methods for disrupting pathological aggregation and / or mis-localization of TDP-43 in the brain / CNS have been developed. Compositions including engineered helical polypeptides that bind TDP-43's amyloidogenic core but resist β-sheet conversion are provided. In some forms, the engineered polypeptides include peptide degradation motifs (PDM) to enhance proteolytic degradation of aggregates, and / or targeting motifs to direct the peptides to the brain / CNS. Recombinant constructs including nucleic acids expressing or encoding the polypeptides are also provided. Methods of using the engineered peptides to treat or prevent one or more diseases or disorders associated with pathological aggregation and / or mis-localization of TDP-43 in the brain / CNS are also provided. In some forms, the methods treat or prevent ALS or FTD in a subject in need thereof.

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.

The invention relates to the technical field of biology, in particular to a pair of mutually recognized and combined alpha helical peptides and application thereof. Comprising an alpha spiral peptide 1 and an alpha spiral peptide 2, the amino acid sequence of the alpha spiral peptide 1 is shown as SEQ ID No.1, and the amino acid sequence of the alpha spiral peptide 2 is shown as SEQ ID No.2. A pair of alpha helical peptides that can recognize and bind to each other bind to each other, whereby cells bind to each other, and the cells are arranged in a desired manner. Proper material concentration and action time are verified; the form of the formed cell mass block is observed through various microscopes; two models are successfully constructed; the improvement of the cell function through the addition of the 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 discloses an artificially designed antibacterial peptide Amphilysin-K20 and an application of the artificially designed antibacterial peptide Amphilysin-K20. The antibacterial peptide is designed based on an alpha-helix peptide (XXYY) n theoretical template through a'skeleton-two end 'collaborative optimization strategy, the amino acid sequence is GILRKFKKVFKKIKRLWILA, the antibacterial peptide has eight positive charges, and the secondary structure is predicted to be alpha-helix. N-terminal glycine enhances the flexibility of a peptide chain, C-terminal alanine stabilizes a spiral structure, and the peptide has an ordered hydrophilic and hydrophobic interface, so that the membrane targeting effect is facilitated. An in-vitro antibacterial activity experiment shows that the MBC / MIC ratio of the antibacterial peptide to each strain is less than or equal to 2, and the antibacterial peptide belongs to a sterilization type antibacterial peptide and shows the rapid sterilization characteristic; safety evaluation shows that the toxicity to human immortalized keratinocytes below 16 mu g / mL is extremely low, and the hemolysis rate is only 1.39% when the concentration is 16 mu g / mL. The antibacterial peptide can be used for preparing an anti-bacterial infection preparation, can also be applied to antibacterial fields in agriculture and aquaculture such as antibacterial material development, cosmetics, food preservation, animal feed additives and animal and plant disease prevention and treatment, and has efficient antibacterial activity and good biological safety.

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.

The invention discloses a polycyclic peptide library and application thereof, the polycyclic peptide library is constructed based on a DRP skeleton, the DRP skeleton is used for stabilizing N-terminal alpha-helix, and the general formula of the DRP skeleton is as follows: (X) mC (X) 7CP (X) 2C (X) nCP (X) 2C (X) 3CXo (sequence 1). A unique DRP skeleton is designed to be used for establishing a disulfide bond-rich multi-skeleton and polycyclic peptide library with an N-terminal extensible alpha-helix structure, so that the stability of N-terminal alpha-helix is realized on the premise of not introducing non-natural amino acid or excessive chemical modification, and extremely high efficiency is shown in the aspects of disulfide bond pairing and polypeptide folding; the problems that the existing alpha-helical peptide is unstable in structure and reduced in affinity after being separated are solved.

The present invention provides a pentapeptide-derived peptide segment RS for anti-skin aging, which relates to the field of biochemistry. The pentapeptide-derived peptide segment RS sequentially includes an amphiphilic helical peptide segment, a linker peptide segment, and KTTKS from the N-terminus to the C-terminus, wherein (b)x(a)y represents the linker peptide segment; a is an uncharged amino acid; b is a basic amino acid; x and y are independently selected from integers greater than or equal to 2. The present invention unexpectedly finds that the pentapeptide-derived peptide segment RS obtained by connecting the amphiphilic helical peptide segment and KTTKS through the linker peptide with the structure of (b)x(a)y has good hydrophilicity and high skin permeability. Direct local application can significantly increase the expression level of type I collagen, increase the skin thickness, and reduce skin wrinkles, achieving a significant anti-skin aging effect.