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20 results about "HECT domain" patented technology

In molecular biology, the HECT domain is a protein domain found in ubiquitin-protein ligases. The name HECT comes from 'Homologous to the E6-AP Carboxyl Terminus'. Proteins containing this domain at the C terminus include ubiquitin-protein ligase, which regulates ubiquitination of CDC25. Ubiquitin-protein ligase accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester, and then directly transfers the ubiquitin to targeted substrates. A cysteine residue is required for ubiquitin-thiolester formation. Human thyroid receptor interacting protein 12 (TRIP12), which also contains this domain, is a component of an ATP-dependent multisubunit protein that interacts with the ligand binding domain of the thyroid hormone receptor. It could be an E3 ubiquitin-protein ligase. Human ubiquitin-protein ligase E3A interacts with the E6 protein of the cancer-associated Human papillomavirus type 16 and Human papillomavirus type 18. The E6/E6-AP complex binds to and targets the p53 tumour-suppressor protein for ubiquitin-mediated proteolysis.

Method of predicting response to treatment

The present invention provides a method of predicting the outcome of a treatment of a cancer or a metabolism-related disease in a subject, the treatment comprising administering to the subject a complex comprising a polypeptide having a naturally occurring alpha-lactalbumin sequence, or a functional variant thereof; or a peptide comprising up to 50 amino acids of the alpha-helical domain of the polypeptide; and a fatty acid or lipid or a salt thereof; wherein the method comprises the steps of: a) evaluating the regulation of cancer genes in the subject after administration of the complex, and b) correlating the regulation of the genes to the outcome of the treatment wherein the positive outcome of the treatment is negatively correlated to the level of regulation of those genes.
Owner:LINNANE PHARMA AB

Bioparticles for the expression of multimeric proteins

PCT designated stageWO2025255685A1Allergen ingredientsImmunoglobulinsBiological particlesCoiled coil
The present invention pertains to specific bioparticules at the surface of which are expressed multimeric protein. The bioparticles according to the present invention comprise an envelope consisting of a plasma membrane; and at least one type I or II transmembrane fusion protein anchored in said membrane, said fusion protein comprising successively a) a first monomer of a multimeric protein of interest, b) a coiled-coil domain or oligomerization sequence; and c) a domain for anchoring in the plasma membrane, consisting of a transmembrane segment and a cytosolic segment. Fragments a) and b) are exposed at the surface of the bioparticle, and fragment a) is bound to a second monomer of said multimeric protein by means of a bond which is not a peptide bond. The bioparticles according to the present invention can be used in therapy such as immunotherapy. The present invention also pertains to methods for producing such bioparticles.
Owner:ANGANY GENETICS

Fusion proteins for affinity capture

A fusion protein comprising at least one first polypeptide moiety and at least one second polypeptide moiety wherein the first polypeptide moiety is a single-chain polypeptide capable of binding to a target entity and the second polypeptide moiety is a stabilizing polypeptide and comprises a single-chain alpha-helix-containing domain, wherein the second polypeptide moiety has no binding affinity for the target entity. The presence of the second polypeptide moiety may improve at least one property of the fusion protein as compared to the property of the first polypeptide moiety alone, where the improved property is selected from the group consisting of: alkaline stability, recombinant protein expression, and coupling to a vector.
Owner:CYTIVA BIOPROCESS R&D AB

Engineered Luciferases and Luciferin Substrates

PendingUS20260250737A1LuciferinNucleic acid detection
The present disclosure provides a protein having luciferase activity, comprising the secondary structure arrangement H1-L1-H2-L2-B1-L3-B2-L4-H3-L5-B3-L6-B4-L7-B5-L8-B6, wherein (i) “H” is a helical domain, “L” is a loop domain, and “B” is a beta strand domain, wherein the B5 domain is at least 11, 12, 13, or 14 amino acids in length and residue 11 of the B5 domain is F, Y, or L; and the B4 domain is at least 12 amino acids in length and residue 10 of the B4 domain is F, Y, L, I, K or M; and / or residue 12 of the B4 domain is F, L, R, D, M, Q or V; (ii) the H1 domain is at least 18 or 19 amino acids in length; residue 9 of the H1 domain is T, S, H, R, C, L, D, V, A, Q, G, E, K, I, N or M; (iii) the B3 domain is at least 6, 7, 8, 9, or 10 amino acids in length and residue 1 of the B3 domain is W or H; (iv) the B4 domain is at least 12 amino acids in length and residue 10 of the B4 domain is F, Y, L, I, K or M; or (v) the B4 domain is at least 12 amino acids in length and residue 12 of the B4 domain is L, R, D, M, Q or V. Additional proteins disclosed herein are exemplified in the claims. Also provided herein are luciferase substrates, assay buffers, and kits comprising one or more of a protein having luciferase activity or a nucleic acid encoding the protein, an assay buffer, and a luciferase substrate.
Owner:MONOD BIO INC

An antimicrobial peptide with two domains

The present invention relates to the field of antimicrobial peptide technology, and in particular to an antimicrobial peptide with a double domain. Mesorhizobium A new AMP sequence with two domains was identified from the protein sequence of the plant (Eubacterium sp.). Independent studies of the β-sheet and α-helical domains revealed for the first time that both domains of a dual-domain antimicrobial peptide have the potential to independently exert antimicrobial activity. The β-sheet region has the potential to inhibit microbial film formation and eliminate mature microbial films, exhibiting particularly significant antimicrobial activity against fungi, but less potent antimicrobial activity against bacteria, potentially reducing damage to the intestinal microbiota. This invention provides new insights and experimental basis for the design of ultrashort antimicrobial peptides and holds broad application prospects.
Owner:GUIZHOU MEDICAL UNIV

Peptide inhibitors of focal adhesion kinase activity and uses thereof

This disclosure provides peptides which have an affinity for the focal adhesion targeting (FAT) domain of focal adhesion kinase (FAK). In particular, the peptides are modified and derived from the sequence of the LD2 alpha helical domain of paxillin (e.g., LD2 peptides), the LD4 domain of paxillin (e.g., LD4 peptides), and CD8 peptides. These peptides are capable of blocking an interaction between paxillin and FAK, thereby inhibiting FAK activity related to FAK-paxillin interaction. The invention further provides uses for such peptides as therapeutics for the treatment of cancer and other diseases characterized with FAK activity and / or expression (e.g., fibrosis).
Owner:THE ARIZONA BOARD OF REGENTS ON BEHALF OF THE UNIV OF ARIZONA

Combined markers for predicting efficacy of targeted drugs for primary liver cancer and application thereof

The present application relates to the field of medical diagnosis, and provides a combined marker for predicting the curative effect of target immune drug for primary liver cancer and application thereof, wherein the combined marker is folate receptor gamma gene FOLR3, stratified protein gene SFN and coiled-coil domain containing 9 gene CCDC9 derived from peripheral blood leukocyte mRNA.The present application performs combined detection based on multiple peripheral blood leukocyte markers, and compared with a single molecular marker, can reduce errors caused by individual expression difference of a single index to some extent, so that the detection result is more accurate.The curative effect prediction model constructed based on detection of peripheral blood leukocyte mRNA level change can specifically recognize and detect in the early stage of tumor formation, has high sensitivity and high specificity, provides an important means for reasonable use of target immune drug for liver cancer patients sensitive or resistant to target immune drug, and has great significance for effective treatment of liver cancer in China.
Owner:HANGZHOU NORMAL UNIVERSITY

Engineered luciferases and luciferin substrates

The present disclosure provides a protein having luciferase activity comprising a secondary structural arrangement H1-L1-H2-L2-B1-L3-B2-L4-H3-L5-B3-L6-L4-L7-L5-L8-B6 wherein (i) "H" is a helical domain, "L" is a loop domain, and "B" is a beta chain domain wherein the length of the B5 domain is at least 11, 12, 13, or 14 amino acids, and wherein "L" is a cyclic domain, and "B" is a beta chain domain. And residue 11 of the B5 domain is F, Y or L; and the length of the B4 domain is at least 12 amino acids, and the residue 10 of the B4 domain is F, Y, L, I, K or M; and / or residue 12 of the B4 domain is F, L, R, D, M, Q or V; (ii) the H1 domain is at least 18 or 19 amino acids in length; the residue 9 of the H1 domain is T, S, H, R, C, L, D, V, A, Q, G, E, K, I, N or M; (iii) the length of the B3 domain is at least 6, 7, 8, 9 or 10 amino acids, and the residue 1 of the B3 domain is W or H; (iv) the length of the B4 domain is at least 12 amino acids, and the residue 10 of the B4 domain is F, Y, L, I, K or M; or (v) the length of the B4 domain is at least 12 amino acids, and the residue 12 of the B4 domain is L, R, D, M, Q, or V. Additional proteins disclosed herein are illustrated in the claims. Also provided herein are luciferase substrates, assay buffers, and kits comprising one or more of a protein having luciferase activity or a nucleic acid encoding the protein, an assay buffer, and a luciferase substrate.
Owner:MONOD BIO INC

Recombinant human collagen type III and preparation method and application thereof

The present application relates to a kind of recombinant human type III collagen and its preparation method and application, belong to the field of bioengineering technology.The amino acid sequence of the recombinant human type III collagen described in the present application is as shown in SEQ ID No.7, is through the directional arrangement of five characteristic triple helix domain and the expansion of polymerization, combined with high-density fermentation process of Pichia pastoris, successfully break through the technical barrier of 4.5g / L target protein concentration.The present application research shows that the recombinant protein at 0.5% concentration not only maintains more than 80% cell viability, more exhibits significant synergistic effect-promote fibroblast migration rate to increase more than 29% compared with blank control group, keratinocyte proliferation rate increases 40.62%, adhesion rate increases 6.53%, provides innovative solution for developing new collagen product with high-efficiency expression and multiple biological activities.
Owner:DONGGUAN EVERON HEALTHCARE CO LTD

Triplex terminators for efficient RNA trans-splicing

A nucleic acid trans-splicing molecule is provided that can replace an exon carrying a defect or mutation that causes an ocular disease in a target mammalian ocular gene with an exon having a naturally occurring sequence and free of the defect or mutation. The trans-splicing molecule includes a 3' transcription terminator domain that enhances the efficiency of trans-splicing. The 3' TTD comprises a triple helix domain and a tRNA-like domain.
Owner:THE TRUSTEES OF THE UNIV OF PENNSYLVANIA

Combined marker for predicting curative effect of primary hepatocellular carcinoma target-immune drug and application of combined marker

The invention relates to the field of medical diagnosis, and provides a combined marker for predicting the curative effect of a primary hepatocellular carcinoma target-free drug and application of the combined marker, and the combined marker is a folate receptor gamma gene FOLR3 derived from peripheral blood leucocyte mRNA, a layered protein gene SFN and a coiled-coil domain protein 9 gene CCDC9. According to the invention, combined detection is carried out based on a plurality of peripheral blood leucocyte markers, and compared with a single molecular marker, errors caused by individual expression difference of a single index can be reduced to a certain extent, so that the detection result is more accurate. The curative effect prediction model constructed based on detection of peripheral blood leucocyte mRNA level change can perform specific recognition detection in the initial stage of tumor formation, has high sensitivity and high specificity, and provides an important means for reasonable medication of hepatocellular carcinoma patients sensitive or resistant to target-free drugs. The important significance is realized on the effective treatment of the hepatocellular carcinoma in China.
Owner:HANGZHOU NORMAL UNIVERSITY

Chimeric recombinant collagen and preparation method and application thereof

The application belongs to the technical field of recombinant proteins, and particularly relates to a chimeric recombinant collagen protein and a preparation method and application thereof. The amino acid sequence of the recombinant collagen protein is shown as SEQ ID NO. 1, and the recombinant collagen protein comprises five functional structures of an intracellular domain, an MMP-2 enzyme cutting domain, a fiber domain, an extracellular domain and a helical domain. The core active fragments are selected from human collagen XVII and human collagen III. The recombinant collagen protein is expressed by a recombinant plasmid through a host cell. The recombinant collagen protein not only retains the transmembrane characteristics and the collagen adhesion characteristics, but also realizes efficient expression of the recombinant collagen protein, enhances skin elasticity, and has an anti-wrinkle effect. Meanwhile, the MMP-2 enzyme cutting domain can provide a microenvironment response site, and can be used in the fields of skin care products, wound repair materials and functional drug carriers.
Owner:SHANDONG D-NUTRIMEC BIOMEDICAL CO LTD

A short peptide mimicking the n-terminal of rhoe, derivatives and pharmaceutical use thereof in the treatment of cardiac hypertrophy

This invention discloses a short peptide and its derivatives that mimic the N-terminus of RhoE, and their pharmaceutical applications in the treatment of myocardial hypertrophy, belonging to the field of biomedical technology. This short peptide precisely mimics the amino acid sequence from position 1 to 20 of RhoE, specifically binding to the WW domain of WWP2 and competitively blocking the interaction between the N-Loop and C-Loop of its HECT domain. This causes the WWP2 conformation to change from a self-inhibited "closed" state to an activated "open" state, activating E3 ligase activity. The short peptide retains its binding ability to the cardiomyocyte membrane cavernin CAV3, allowing it to efficiently enter the cardiomyocyte cytoplasm via the cavernin endocytosis pathway, overcoming the deficiency of traditional drugs in clearing intracellular pathogenic proteins. Peptide derivatives constructed by fusing transmembrane peptides such as TAT ​​and T7 further improve intracellular delivery efficiency. Experiments have demonstrated that this short peptide and its derivatives can significantly promote WWP2 self-ubiquitination, enhance cardiomyocyte autophagic flux, clear intracellular pathogenic proteins, and effectively inhibit cardiomyocyte hypertrophy, making it suitable for the preparation of anti-myocardial hypertrophy drugs.
Owner:THE SIXTH AFFILIATED HOSPITAL OF XINJIANG MEDICAL UNIV

A recombinant elastin and its preparation method and application

This invention relates to a recombinant elastin-like protein, its preparation method, and its applications, belonging to the field of biomacromolecule technology. This invention provides a recombinant elastin-like protein comprising an elastin-like motif and a type III collagen functional motif; the amino acid sequence of the elastin-like motif is VPGXG, where X in VPGXG is any one of H, R, K, I, F, L, W, A, M, C, N, V, G, S, Q, Y, D, E, and T; the amino acid sequence of the type III collagen functional motif is shown in SEQ ID NO.1. This invention provides a recombinant elastin-like protein that fuses a collagen motif and an elastin motif with a triple-helix domain that promotes cell adhesion activity, possessing thermosensitive properties, pH-responsive characteristics, and gelling properties, and exhibiting anti-aging, anti-inflammatory, skin barrier repair, and soothing effects.
Owner:完美(广东)日用品有限公司 +2

Recombinant elastin-like protein as well as preparation method and application thereof

The invention is a divisional application of an invention patent application of which the application date is November 7, 2024, the application number is 202411581372.8, and the invention name is'a recombinant elastin-like protein as well as a preparation method and application thereof '. The invention relates to a recombinant elastin-like protein as well as a preparation method and application thereof, and belongs to the technical field of biomacromolecules. The invention provides a recombinant elastin-like protein. The recombinant elastin-like protein comprises an elastin-like protein motif and a collagen III functional motif, the amino acid sequence of the elastin-like motif is VPGXG; the amino acid sequence of the III type collagen functional motif is as shown in SEQ ID NO. 1. The invention provides the recombinant elastin-like protein which is fused with the collagen motif and the elastin motif of the triple helix structural domain with the activity of promoting cell adhesion, and the recombinant elastin-like protein has the temperature-sensitive characteristic, the pH response characteristic and the gel characteristic, and has the effects of resisting aging, resisting inflammation and repairing the skin barrier.
Owner:完美(广东)日用品有限公司 +2

A recombinant human type XVII collagen, its preparation method and application

This invention relates to a recombinant human type XVII collagen, its preparation method, and its applications, belonging to the field of bioengineering technology. The amino acid sequence of the recombinant human type XVII collagen is shown in SEQ ID No. 4. It is formed by constructing recombinant monomers through the directional arrangement of two characteristic triple-helix domains, and then further formed by the tandem connection of eight monomer units. The collagen retains its natural active sites while enhancing its mechanical strength. Combined with high-density fermentation technology using Pichia pastoris, high-expression, high-purity recombinant collagen was successfully obtained. This recombinant protein not only maintains over 85% cell viability at a concentration of 0.5%, but also exhibits multiple biological activities—promoting fibroblast migration rate by over 57%, keratinocyte proliferation rate by 20.97%, and showing significant hair growth effects. This invention provides an innovative solution for developing novel collagen products with both high-efficiency expression and multiple biological activities.
Owner:DONGGUAN EVERON HEALTHCARE CO LTD

Extracellular matrix polymer protein as well as preparation method and application thereof

The invention relates to the technical field of biology, in particular to extracellular matrix polymer protein and a preparation method and application thereof. The invention also relates to a recombinant protein composition, a polynucleotide composition, a carrier composition, a recombinant cell composition and an active additive or preparation used in the fields of tissue engineering, pharmacy or beauty and skin care related to the extracellular matrix multimeric protein. The extracellular matrix polymer protein comprises a first subunit and a second subunit, the first subunit comprises a first coiled-coil domain and at least one extracellular matrix protein fragment; the second subunit comprises a second coiled-coil domain and at least one extracellular matrix protein fragment; the first subunit and the second subunit are non-covalently bound via the first coiled helical domain and the second coiled helical domain. The extracellular matrix polymer protein overcomes at least one of the defects of rigid multi-module assembly structure, insufficient activity retention and low yield after fusion of the traditional artificially prepared extracellular matrix protein.
Owner:苏州臻泰生物科技有限公司

Therapy

The present invention relates to a complex comprising a polypeptide having a sequence of a naturally occurring alpha-lactalbumin, or a functional variant thereof; or a peptide of up to 50 amino acids comprising an alpha-helical domain of said polypeptide; and a fatty acid or lipid or salt thereof for use in therapy for the treatment of metabolic-related disorders, particularly metabolic-related disorders that are modulated by, or otherwise affected by the leptin and / or adiponectin pathway.
Owner:LINNANE PHARMA AB

Recombinant human XVII type collagen as well as preparation method and application thereof

The invention relates to recombinant human XVII type collagen as well as a preparation method and application thereof, and belongs to the technical field of bioengineering. The amino acid sequence of the recombinant human XVII type collagen is shown as SEQ ID No.4, and the recombinant human XVII type collagen is formed by constructing a recombinant monomer through directional arrangement of two characteristic triple helical structural domains and further connecting eight monomer units end to end in series; the collagen not only retains natural active sites, but also enhances the mechanical strength. And the recombinant collagen with high expression quantity and high purity is successfully obtained by combining a pichia pastoris high-density fermentation technology. The recombinant protein not only keeps more than 85% of cell activity at the concentration of 0.5%, but also shows multiple biological activities, the fibroblast migration rate is promoted to be improved by over 57%, the keratinocyte proliferation improvement rate is 20.97%, and the recombinant protein has a remarkable hair growth effect; the invention provides an innovative solution for developing a novel collagen product with efficient expression and multiple biological activities.
Owner:DONGGUAN EVERON HEALTHCARE CO LTD

Recombinant human III-type collagen as well as preparation method and application thereof

The invention relates to recombinant human III-type collagen as well as a preparation method and application thereof, and belongs to the technical field of bioengineering. The amino acid sequence of the recombinant human III-type collagen is shown as SEQ ID No.7, and the technical barrier of 4.5 g / L target protein concentration is successfully broken through by directional arrangement and multimerization expansion of five characteristic triple helical structural domains in combination with a pichia pastoris high-density fermentation process. Researches show that the recombinant protein not only keeps more than 80% of cell activity at the concentration of 0.5%, but also shows remarkable synergistic effects, namely promoting the migration rate of fibroblasts to be increased by more than 29% compared with a blank control group, increasing the proliferation rate of keratinocytes by 40.62%, increasing the adhesion rate by 6.53% and increasing the survival rate of the keratinocytes. An innovative solution is provided for developing a novel collagen product with efficient expression and multiple biological activities.
Owner:DONGGUAN EVERON HEALTHCARE CO LTD