34 results about "Hydrophobic residue" patented technology

The invention relates to methods for the stabilisation of cytokines and to cytokines generated by such methods. The methods of the invention involve mutating the amino acid sequence of a cytokine so as to remove solvent-exposed hydrophobic residues, and/or mutating the amino acid sequence of the cytokine so as to stabilise one or more secondary structure elements in the molecule. These steps have the effect of destabilsing intermediates that are formed during the folding process, relative to the stability of the cytokine in its naturally folded state, so increasing the yield of the cytokine as produced in vitro.

Self assembling peptides and peptidomimetics can be utilized for the treatment and support of disorders associated with leaky or damaged tight junction and weak, diseased, or injured extracellular matrix. The self-assembling materials generally have alternating hydrophilic or hydrophobic residues or hydrophobic and/or hydrophilic sections which allow the material to react or interact with the glycoproteins found in the ECM. Diseases in which treatment with these materials applied to or near the site in need of treatment include diabetic retinopathy, sepsis, burns, and certain neurodegenerative diseases such as Parkinson's and Alzheimer's. The formulations can be administered by injection, spraying, topically or by catheter or via a wound dressing or other material to which it is applied and then applied to the site in need of treatment.

The invention encompasses hexapeptides consisting of alternating hydrophobic residues (B) at positions 2, 4, and 6, hydrophilic, hydrophilic, charged residues (X) at positions 1 and 3, and a naphthylalanine (Nal), an aliphatic or aromatic residue (O) at position five, represented generally by the formula XBXBOB, which exhibit antimicrobial activity against infections caused by a variety of pathogens. These pathogens may include gram positive or negative bacteria, acid-fast bacteria such a mycobacteria, parasites, dermatophytes, or fungal pathogens. Typical fungal pathogens include Candida albicans and typical dermatophytes include Trichophyton rubrum and Trichophyton mentagrophytes. The hexapeptides of the present invention exhibit antifungal activity, antibacterial activity, desirable stability, and lack toxicity to the mammal receiving treatment.

It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by masking the site with a compound that prevents IgE binding or by altering as little as a single amino acid within the protein, most typically a hydrophobic residue towards the center of the IgE binding epitope, to eliminate IgE binding. The method allows the protein to be altered as minimally as possible, other than within the IgE-binding sites, while retaining the ability of the protein to activate T cells, and, in some embodiments by not significantly altering or decreasing IgG binding capacity. The examples use peanut allergens to demonstrate alteration of IgE binding sites. The critical amino acids within each of the IgE binding epitopes of the peanut protein that are important to immunoglobulin binding have been determined. Substitution of even a single amino acid within each of the epitopes led to loss of IgE binding. Although the epitopes shared no common amino acid sequence motif, the hydrophobic residues located in the center of the epitope appeared to be most critical to IgE binding.

Disclosed is a new structural class of amphiphilic molecules which incorporate a hydrophilic material or polymer attached, at spatially distinct sites, to at least two hydrophobic residues. Certain of the amphiphilic molecules comprise a plurality of hydrophobic moieties. All such amphiphilic molecules have a common structural motif and, in contact with water, display surface activity and self-assemble into multimolecular aggregates and liquid crystalline phases. Also disclosed are enhanced stability liposomes that incorporate such amphiphilic molecules via unique interactions, and methods of using such formulations in a variety of applications including drug delivery, nutrition, bio-diagnostics, cosmetics, blood products and related applications.

The invention includes a streptavidin mutein having at least one mutation chosen to cause one or more of steric hindrance, charge repulsion, or improvement of solubility by changing interfacial hydrophobic residues to less hydrophobic or hydrophilic residues. The mutein may exist in monomeric form even in the presence of biotin, and reversibly binds to biotin. The invention also includes polynucleotides encoding such muteins, expression systems and host cells for producing such muteins. The invention also includes a method of capturing biotinylated molecules using the muteins of the invention.

The invention relates to dendrobium officinale oligosaccharide, a dendrobium officinale oligosaccharide derivative and a preparation method and application of the dendrobium officinale oligosaccharide and the dendrobium officinale oligosaccharide derivative, and the main technology is that the dendrobium officinale oligosaccharide contains 3-9 glycoside residues and has glucose residues at a non-reducing end; the derivative is obtained through substitution at the non-reducing end with hydrophobic residues . The invention further provides a preparation method and application of the two compounds. The invention has the beneficial effects that the dendrobium officinale oligosaccharide with the purity of more than or equal to 99% is prepared from the dendrobium officinale for the first time, the structure, the anti-aging activity effect and the immune regulation effect of the dendrobium officinale oligosaccharide are defined, and the dendrobium officinale oligosaccharide is found to be capable of well inhibiting collagenase and also has certain activity on TNF-alpha and IL-6; the method can be applied to the fields of medicine, food and daily necessity development.

The invention includes a streptavidin mutein having at least one mutation chosen to cause one or more of steric hindrance, charge repulsion, or improvement of solubility by changing interfacial hydrophobic residues to less hydrophobic or hydrophilic residues. The mutein may exist in monomeric form even in the presence of biotin, and reversibly binds to biotin. The invention also includes polynucleotides encoding such muteins, expression systems and host cells for producing such muteins. The invention also includes a method of capturing biotinylated molecules using the muteins of the invention.

The invention describes factor VIII molecules with reduced capacity to elicit activation of NKT cells for use in the treatment of congenital and/or acquired haemophilia A and in bleeding disorders. Said factor VIII molecule is obtainable by:

• • a. identification of at least one NKT cell epitope wherein said epitope comprises hydrophobic aminoacid residues in position P1 and/or P7
  • b. modification of said epitope(s) by eliminating at least one hydrophobic aminoacid residues in position P1 and/or P7, substituting at least one hydrophobic aminoacid residue in position P1 and/or P7 with a non-hydrophobic residue, or adding a non-hydrophobic residue in position P1 and/or P7.

Focused library synthesis and medicinal chemistry on an oxadiazole-isopropylamide core proteasome inhibitor provided the lead compound that strongly inhibits CT-L activity. Structure activity relationship studies indicate the amide moiety and two phenyl rings are sensitive toward synthetic modifications. Only para-substitution in the A-ring was important to maintain potent CT-L inhibitory activity. Hydrophobic residues in the A-ring's para-position and meta-pyridyl group at the B-ring significantly improved inhibition. The meta-pyridyl moiety improved cell permeability. The length of the aliphatic chain at the para position of the A-ring is critical with propyl yielding the most potent inhibitor, whereas shorter (i.e. ethyl, methyl or hydrogen) or longer (i.e. butyl, propyl and hexyl) chains demonstrating progressively less potency. Introduction of a stereogenic center next to the ether moiety (i.e. substitution of one of the hydrogens by methyl) demonstrated chiral discrimination in proteasome CT-L activity inhibition (the S-enantiomer was 35-40 fold more potent than the R-enantiomer).

The invention discloses a maltose functionalized nanometer composite material based on ion complementation type peptide self-assembly and a preparation method and application of the composite material. By modifying self-assembly, on the surfaces of SiO2@Fe3O4, C@Fe3O4 and other nanometer materials, of the ion complementation type peptide with alternating hydrophilic and hydrophobic residues on maltose, the stable maltose functionalized nanometer composite material is obtained. The composite material can selectively enrich glycopeptides in standard glycoprotein and biological sample enzymolysisliquid, the enrichment efficiency is high, the selectivity is high, the detection limit is low, the performance is stable, and the composite material can be reused. The composite material is simple in preparation method, mild in condition, green, free of toxin and capable of being used for one-step surface functionalization of various nanometer enrichment materials.

The present invention relates to a novel bidentate motif that is composed of two adjacent residues of tyrosine and serine which have been found to be involved in the binding of crucial cytoplasmic proteins which are involved in cell signalling pathways. In some cases, the cytoplasmic proteins are ubiquitous proteins involved in cell signalling pathways that may include mitogenesis, transformation and survival.

The bidentate motif may have a sequence alignment

wherein X is any residue, Y is tyrosine, S/T is serine or threonine and Ψ is a hydrophobic residue or an equivalent thereof. Preferably the residues are Tyr577 and Ser585 of the common βc of the GM-CSF/IL-5/IL-3 receptor.

The invention relates to the technical field of medicines, in particular to a xanthine oxidase inhibitor. A tannic acid carbon dot and tannic acid mixture which has good water solubility, low toxicity and biocompatibility and has a xanthine oxidase inhibition effect is used as a xanthine oxidase inhibitor, and the tannic acid carbon dot and the tannic acid are combined with hydrophobic residues of xanthine oxidase to form hydrogen bonds or generate a hydrophobic effect; and when being inserted into hydrophobic gaps of the xanthine oxidase, the xanthine oxidase occupies a catalytic activity center, and competes with a substrate xanthine to be combined with an active site of the xanthine oxidase, so that the substrate is prevented from entering, and the activity of the xanthine oxidase is reduced. In-vitro and in-vivo animal experiment results show that the xanthine oxidase inhibitor disclosed by the invention can be equivalent to hyperuricemia drugs in the prior art, is low in toxicity, and can be applied to health-care foods or drugs for preventing and treating hyperuricemia.

This invention describes analogues of human parathyroid hormone which have increased activities in bone restoration, and increased bioavailabilities. The peptides described are derivatives of hPTH-(1-31) which are cyclized for example, by formation of Lactams between either Glu<22> and Lys<26> or Lys<26> and Asp<30>. In addition, the natural Lys<27> may be substituted by either a Leu or other hydrophobic residues, such as Ile, norleucine, Met, Val, Ala, Trp, or Phe. Typically, these analogues have enhanced abilities to stimulate adenylyl cyclase in rat osteosarcoma cells, and show increased activities in bone restoration, using the ovariectomized rat model. The analogues also show enhanced activities and bioavailabilities, as demonstrated by their hypotensive effects in the rat. An assay which correlates hypotensive activity with osteogenic activity is also described.

Provided herein are methods directed to engineering monoclonal antibodies and antibody variants to improve stability and their production in culture. Specifically, the monoclonal antibodies can be engineered at heavy chain residue 56 (AHo numbering) to a glycine, alanine, or serine, and/or engineered at position 80 (AHo) to be a hydrophobic residue such as alanine, isoleucine, phenylalanine, leucine, methionine, or valine.