34 results about "Hydrophobic residue" patented technology

The invention encompasses hexapeptides consisting of alternating hydrophobic residues (B) at positions 2, 4, and 6, 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 as 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.

A novel class of antimicrobial polymeric agents, which include a plurality of amino acid residues, such as positively charged amino acid residues, and at least one hydrophobic residue linking therebetween, such as an omega-amino-fatty acid residue, designed to exert antimicrobial activity while being stable, non-toxic and avoiding development of resistance thereto, and a process of preparing same, are disclosed. Further disclosed are pharmaceutical compositions containing same and a method of treating medical conditions associated with pathological microorganisms, a medical device, an imaging probe and a food preservative utilizing same. Further disclosed are conjugates of an amino acid residue and a hydrophobic moiety residue and a process of preparing same.

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 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.

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.

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 relates to the biotechnology field, specifically relates to an improvement method of natural anticancer peptide. The method comprises the design improvements at two stages by use of natural polypeptide as a template; in the design improvement at the first stage, a series of polypeptide derivatives are obtained by changing the percentage of polypeptide net charge and the hydrophobic residue in the polypeptide; in the design improvement at the second stage, the variety and the number of the screened polypeptide amino acid residue are unchanged, only the primary amino acid sequence is changed, so that the alpha-helix in the high-level structure is located at different positions or disappeared to obtain the series of polypeptide again. The anticancer peptide prepared by use of the method disclosed by the invention is not only high in anticancer property, but also small in toxicity and safer to the human body.

The invention relates to a Dendrobium officinale oligosaccharide, a Dendrobium officinale oligosaccharide derivative and a preparation method and application thereof. The main technology is that the Dendrobium officinale oligosaccharide contains 3-9 glycoside residues and has glucose at the non-reducing end residue; its derivatives are obtained by substituting hydrophobic residues at the non-reducing end, and the preparation method and application of the two are also provided. The beneficial effects of the present invention are as follows: for the first time, Dendrobium candidum oligosaccharides with a purity ≥ 99% were prepared from Dendrobium candidum, and the structure, anti-aging activity and immune regulation of Dendrobium candidum oligosaccharides were clarified, and it was found that it can well inhibit Collagenase also has certain activity on TNF-α and IL-6; it can be used in medicine, food, daily necessities development and other fields.

The invention discloses a maltose functional nanometer material based on ion-complementary peptide self-assembly, a preparation method and an application thereof. In the present invention, the ion-complementary peptide with alternate arrangement of hydrophilic and hydrophobic residues modified on maltose is placed on SiO 2 @Fe 3 o 4 and C@Fe 3 o 4 Self-assembly on the surface of other nanomaterials to form stable maltose-functionalized nanocomposites. The composite material of the invention can selectively enrich standard glycoproteins and glycopeptides in enzymatic hydrolysis solutions of biological samples, has high enrichment efficiency, good selectivity, low detection limit, stable performance and can be reused. The preparation method of the composite material is simple, the conditions are mild, green and non-toxic, and can be used for one-step functionalization of the surface of various nano-enriched materials.