79 results about "Aspartic acid residue" patented technology

A compound represented by the following general formula (I), wherein R¹ and R² represent a hydrocarbon group having 1 to 26 carbon atoms, preferably a linear or branched alkyl group, R³ represents a hydrocarbon group having 7 to 10 carbon atoms, preferably a linear or branched alkyl group, n represents 1 or 2 provided that the acidic amino acid residue in the molecule is L-aspartic acid residue when n is 1 and said acidic amino acid residue is L-glutamic acid residue when n is 2, and a gelling agent for an oil comprising said compound

The invention is directed to methods of treatment of Alzheimer's disease and other tauopathies, via the administration of antibodies having specificity to abnormal forms of tau protein, the antibodies showing no binding and/or reactivity to a normal tau protein and being administered under conditions and in amounts effective to prevent or treat Alzheimer's disease or other tauopathies. In certain embodiments, the antibodies are selective for soluble truncated tau protein truncated at (i) its C-terminus after the glutamic acid residue Glu391, or (ii) at the aspartic acid residue Asp421, or (iii) at its N-terminus at the aspartic acid residue Asp13, or (iv) a combination of (i)-(iii). Further aspects of the invention are directed to the administration of an immunogen comprising an abnormal tau, preferably a soluble truncated tau.

The invention is directed to methods of treatment of Alzheimer's disease and other tauopathies, via the administration of antibodies having specificity to abnormal forms of tau protein, the antibodies showing no binding and/or reactivity to a normal tau protein and being administered under conditions and in amounts effective to prevent or treat Alzheimer's disease or other tauopathies. In certain embodiments, the antibodies are selective for soluble truncated tau protein truncated at (i) its C-terminus after the glutamic acid residue Glu391, or (ii) at the aspartic acid residue Asp421, or (iii) at its N-terminus at the aspartic acid residue Asp13, or (iv) a combination of (i)-(iii). Further aspects of the invention are directed to the administration of an immunogen comprising an abnormal tau, preferably a soluble truncated tau.

The present invention relates to a method for recombinant production of a C1q protein or a variant of the C1q protein, in which the protein is recovered from an in vitro culture of cells expressing a C1qA subunit or a variant of the C1qA subunit, a C1qB subunit or a variant of the C1qB subunit, and a C1qC subunit or a variant of the C1qC subunit, in which at least one of the subunits or subunit variants also has at the N-terminus or C-terminus a sequence of amino acids of at least six residues, at least 40% of which are glutamic acid and/or aspartic acid residues.

The present invention provides substituted humanized, chimeric or human anti-CD20 antibodies or antigen binding fragments thereof and bispecific antibodies or fusion proteins comprising the substituted antibodies or antigen binding fragments thereof. The antibodies, fusion proteins or fragments are useful for treatment of B-cell disorders, such as B-cell malignancies and autoimmune diseases, as well as GVHD, organ transplant rejection, and hemolytic anemia and cryoglobulinemia. Amino acid substitutions, particularly substitution of an aspartate residue at Kabat position 101 of CDR3 VH (CDRH3), result in improved therapeutic properties, such as decreased dissociation rates, improved CDC activity, improved apoptosis, improved B-cell depletion and improved therapeutic efficacy at very low dosages. Veltuzumab, a humanized anti-CD20 antibody that incorporates such sequence variations, exhibits improved therapeutic efficacy compared to similar antibodies of different CDRH3 sequence, allowing therapeutic effect at dosages as low as 200 mg or less, more preferably 100 mg or less, more preferably 80 mg or less, more preferably 50 mg or less, most preferably 30 mg or less of naked antibody when administered i.v. or s.c.

The present invention provides a modified biotin-binding protein comprising an amino acid sequence represented by SEQ ID NO: 2 or its modified sequence and having a biotin-binding activity and replacement selected from the group consisting of:

• • 1) replacement of the 36th serine residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond;
  • 2) replacement of the 80th tryptophan residue of SEQ ID NO: 2 with a hydrophilic amino acid residue;
  • 3) replacement of the 116th aspartic acid residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond;
  • 4) replacement of the 46th proline residue of SEQ ID NO: 2 with a threonine, serine, or tyrosine residue and replacement of the 78th threonine residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond;
  • 5) replacement of the 46th proline residue of SEQ ID NO: 2 with a threonine, serine, or tyrosine residue and replacement of the 116th aspartic acid residue of SEQ ID NO: 2 with an amino acid that does not form a hydrogen bond; and
  • 6) replacement of the 46th proline residue of SEQ ID NO: 2 with a threonine, serine, or tyrosine residue, replacement of the 78th threonine residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond, and replacement of the 116th aspartic acid residue of SEQ ID NO: 2 with an amino acid that does not form a hydrogen bond.

The invention relates to a group of cyclo-polypeptides capable of combining with autocrine RNAIII activator protein of gold staphylococcus, Steroidal C#-[1]-X#-[1]-H#-[1]-A#-[2]-H#-[1]-A#-[2]-C#-[1], wherein C is natural L-type aminothiopropionic acid residue or its D-type isomer, X is any one of the four natural L-type amino acid residue or its D-type isomers, i.e. glutamine residue (Q), glutacid residue (E), aspartate residue (D), asparagines residue (N), H is L-type histidine residue or its D-type isomer, A is natural L-type aromatic residue or its D-type isomer. The polypeptides can be applied in preparing staphylococcus aureus resistant medicament.

The present disclosure relates to peptide monomers comprising an amphipathic ?-helical peptide, and optionally, at least one T cell epitope peptide; and to dimers and trimers comprising the peptide monomers. The monomeric, dimeric, and trimeric peptides may be conjugated to at least one hapten, wherein the hapten is linked to a lysine or aspartic acid residue of the peptide monomer. These peptide conjugates are useful as vaccine delivery vehicles.

A contrast agent comprising a polypeptide is provided. The polypeptide contains lysine residues and optionally, one or more types of amino acid residues selected from the group consisting of glutamic acid residues and aspartic acid residues, wherein the lysine residues are substituted with a group derived from a steric hindrance molecule; and an image producing entity is present in a range between about 100 units and about 2000 units. Methods for administering the aforementioned contrast agent are also provided.

The emergence of mutations in tyrosine kinases following treatment of cancer patients with molecular-targeted therapy represents a major mechanism of acquired drug resistance. Here, we describe a mutation in the serpentine receptor, Smoothened (SMO), which results in resistance to a Hedgehog (Hh) pathway inhibitor in medulloblastoma. A single amino acid substitution in a conserved aspartic acid residue of SMO maintains Hh signaling, but results in the inability of the Hh pathway inhibitor, GDC-0449, to bind SMO and suppress the pathway. This mutation was not only acquired in a GDC-0449-resistant mouse model of medulloblastoma, but was identified in a Medulloblastoma patient following relapse on GDC-0449. The invention provides screening methods to detect SMO mutations and methods to screen for drugs that specifically modulate mutant SMO exhibiting drug resistance.

The present invention discloses one kind of VIP analog with the amino acid sequence as shown in SEQ ID No. 1, that is, the VIP analog has the VIP amino acid sequence with the arginine residue substituting the aspartic acid residue in the position 8, the arginine residues lysine residues in the positions 15 and 21, and the leucine residue substituting the methionine residue in the position 17. The present invention also discloses the radioactive marker, especially two 18F markers, of the VIP analog, and their preparation process. The VIP analog of the present invention has high metabolic stability and excellent receptor associativity, and the radioactive markers is suitable for use in preparing radioactive developing reagent for detecting in vivo VIP acceptor.

The invention discloses a varied SHV type beta-lactamase, which comes from bacteria and comprises a variant from the following: the 79th alanine residue in amino-acid sequence shown in sequence 2 in the sequence table is substituted by threonine residue, or 101th aspartic acid residue is substituted by histidine residue, or 214th aspartic acid residue is substituted by alanine residue, or 203th serine is substituted by leucine residue. The invention also discloses the gene sequence of the varied SHV type beta-lactamase and the application of the beta-lactamase. The varied SHV type beta-lactamase of the invention is of activity from super-wide spectrum beta-lactamase, provides useful information for developing and preparing anti-medicine gene inspection chip of beta-lactamase, guides the research and development as well as preparation of anti-medicine bacteria antibiotic, and effectively improve the direction-targeting in the use of antibiotic.

Human interferon-ss protein analogs in which the asparagine at position 25, numbered in accordance with native human interferon-ss, is recombinantly replaced with an aspartate residue exhibit a biological activity of human interferon-ss (e.g. IFN-ss 1b) at an increased level relative to IFN-ss 1b. These analogs are obtained by introducing a gene coding for Asp25 IFN-ss into a cell and expressing the recombinant protein. The resulting IFN-ss protein analog is suitable for large scale manufacturing for incorporation in HA-containing or HA-free therapeutics for treatment of diseases including multiple sclerosis. A reduced Lys endoproteinase-C peptide map technique that produces a fingerprint profile for proteins using an enzymatic digest followed by RP-HPLC is also useful in quality control as an ID test for the IFN-ss protein analog products.