430 results about "Inhibitory peptide" patented technology

The present invention provides peptide analogs and peptide mimetics that inhibit pleated sheet formation in amyloid beta-peptide, pharmaceutical compositions thereof and their therapeutic use. The inhibitory peptides possess activity as inhibitors in the formation of amyloid-like deposits and are useful in the treatment of Alzheimer's Disease.

Disclosed are peptides that inhibit the enzymatic activity of tyrosinase, as well as formulations and methods for their use in the reduction of skin pigmentation, and methods of administering the inhibitory peptides in a topical formulation. Peptide sequences disclosed include KFEKKFEK and YRSRKYSSWY.

A method for preparing ACE inhibition peptides from fish skin is provided. The method is prepared with tilapia skin, extracts fish skin albumen from tilapia skin, adapts prolease to hydrolysis through enzyme extinguishing, debitterizing, decolouring, de-flavoring, filtering, ion exchanging and concentrating to obtain fish skin proteolysis liquor, after untruly filter (cutoff molecular mass is 9000Da) the TSP-I, collect high activity component by SephadexG-15 gel chromatography, freeze and dry to obtain high activity ACE inhibition peptides. The invention has important meaning for satisfying integrated utilization of tilapia skin wastes and improving its attachment.

The invention provides peptides that bind Tissue Factor Pathway Inhibitor (TFPI), including TFPI-inhibitory peptides, and compositions thereof. The peptides may be used to inhibit a TFPI, enhance thrombin formation in a clotting factor-deficient subject, increase blood clot formation in a subject, and/or treat a blood coagulation disorder in a subject.

The invention provides methods for designing peptides that inhibit aggregation in target polypeptides. The candidate inhibitory peptidic compounds have an oligomeric sequence that forms energetically-favorable interactions with the amino acid sequence of the steric zipper region of the target protein, and also possess a zipper-disrupting feature that disrupt the peptide stacking at the steric zipper region. This method can be used to obtain inhibitory peptides to disrupt fibril formation involving any protein for which a steric zipper sequence can be identified. The invention also provides inhibitory peptidic compounds, which can be used in pharmaceutical compositions and methods for treating polypeptide aggregation-associated diseases or conditions.

The present invention provides a method for the screening of nucleic acid fragment expression libraries and selecting encoded peptides based upon their ability to modulate the activity of a target protein or nucleic acid and assume conserved conformations compatible with albeit not reiterative of the target protein or nucleic acid. The present invention also provides methods for the diagnosis and treatment of ischemia. The present invention also provides c-Jun dimerization inhibitory peptides and analogues thereof that are useful for treatment of ischemia.

The invention discloses an angiotensin converting enzyme inhibitory peptide, which is characterized by comprising the following amino acid sequences: SEQ NO1: Arg-Leu-Ser-Phe-Asn-Pro, SEQ NO2: Leu-Leu, and SEQ NO3: Ala-Leu-Pro-Met-His-Ile-Arg. The method for preparing the inhibitory peptides comprises the following steps of: (1) preparing lactalbumin concentrated solution; (2) preparing lactalbumin hydrolysis liquid; (3) preparing angiotensin converting enzyme-containing inhibitory peptide concentrated solution; (4) performing separation and purification on the inhibitory peptide-containing concentrated solution through gel chromatography and reverse-phase high-pressure liquid chromatography; and (5) obtaining the product by freeze drying. The invention has the advantages that: three amino acid sequences of the angiotensin converting enzyme inhibitory peptide derived from the lactalbumin are disclosed for the first time, the preparation cost is low and the extraction ratio is high.

The invention discloses a novel orally-effective spirulina source antihypertensive peptide and a preparation method thereof. The antihypertensive peptide is a tripeptide with the sequence of isoleucine-glutamine-proline (Ile-Gln-Pro, IQP). An angiotensin converting enzyme (ACE) inhibitory peptide is prepared by the following steps of: performing enzymolysis on spirulina platensis by adopting alkali protease, and performing ultrafiltration, gel filtration chromatography and secondary reversed phase high-performance liquid chromatography purification. Tests prove that the IQP is a noncompetitive inhibitor of ACE, and can keep good ACE inhibitory activity under digestion of main gastrointestinal protease. The IQP has good antihypertensive effect on essential hypertension rat (SHR) and has great application prospects in medicaments and functional foods for preventing and treating hypertension.

The invention discloses a method for preparing a DPP-IV inhibitory peptide through using hairtail. The method is characterized in that the method comprises the following steps: adding water to hairtail, and rubbing to form a uniform fish flesh pulp; putting the fish flesh pulp in an enzymatic hydrolysis tank, adding endo protease, and carrying out stirring hydrolysis for 4-12h to obtain a hydrolysate; heating to 95-100DEG C, and maintaining the temperature unchanged for 10-15min for enzyme killing; cooling the hydrolysate to 40-60DEG C, adding exoproteinase, and carrying out stirring hydrolysis for 2-8h; heating to 95-100DEG C, and maintaining the temperature unchanged for 10-15min for enzyme killing; centrifuging the obtained enzyme-killed hydrolysate, and taking the obtained supernatant; adding the supernatant to an ultrafilter membrane separator, adjusting the pressure and the interception molecular weight of the ultrafilter membrane to 0.05-0.1MPa and 3000Da respectively, and collecting an ultrafilter membrane permeate liquid; and separating and purifying the DPP-IV inhibitory peptide through adopting an affinity chromatography process. The method has the advantages of simple technology, low production cost and short production period.

Intravitreal administration of a JNK-inhibitory peptide less than 150 amino acids in length, containing at least one D-amino acid, and having (a) a JNK-inhibitory sequence of at least any of SEQ ID NO: 1 and SEQ ID NO: 2, and (b) a transport sequence of at least any of SEQ ID NO: 3 and SEQ ID NO: 4 suppressed spermidine-induced retinal pigment epithelial damage, tunicamycin-induced photoreceptor cell damage, and laser-induced choroidal neovascularization. Thus, the JNK-inhibitory peptide of the present invention is useful for prophylaxis or therapy of a retinal disease. By the use of this JNK-inhibitory peptide, a drug and a method are provided which are capable of preventing or treating a retinal disease even by topical administration to the eye, and use of the JKN-inhibitory peptide for manufacturing the drug is also provided.

The present invention relates to compounds of the Formula I

wherein R¹, R³, R⁵, R⁷, X, Y and U are as defined. Compounds of the Formula I have activity inhibiting production of Aβ-peptide. The invention also relates to pharmaceutical compositions and methods of treating diseases and disorders, for example, neurodegenerative and/or neurological disorders, e.g., Alzheimer's disease, in a mammal comprising compounds of the Formula I.

The invention relates to a tumor inhibitory peptide capable of being specifically bound with PD-1 and an application thereof. The inhibitory peptide can be bound with an extracellular region of a PD-1 protein receptor and can effectively close a PD-1 protein at protein level and cellular level and prevent the PD-1 protein from being bound with a ligand PD-L1. The polypeptide has good biological activity. The polypeptide can be used in tumor immunotherapy alone or combined with an anti-PD-1 monoclonal antibody or other anti-tumor drugs as well as diagnosis and screening of a PD-1 positive tumor patient, namely the polypeptide can be applied to preparation of drugs used for treating tumor and autoimmune diseases.

The invention aims at providing a novel angiotensin-converting enzyme inhibition peptide, namely an ACE inhibition peptide prepared form isochrysis galbana, and with the amino acid sequence of SEQ ID NO:1. The invention provides a preparation method of a high-activity angiotensin-converting enzyme inhibition peptide sourcing from marine microalgae. The current angiotensin-converting enzyme inhibiter mainly comes from food and large macroalgae of laver and the like, and coming from bait microalgae is not reported. The structure of the obtained active peptide with a unique structure is Tyr-Met-Gly-Leu-Asp-Leu-Lys. The structure is novel and has the characteristics of being small in molecular weight and easily absorbed by a human body.

Methods for treating arthritis comprising 14-3-3 antagonists that are capable of specifically binding to extracellularly localized 14-3-3 eta and/or 14-3-3 gamma protein isoforms are provided. In preferred embodiments, the 14-3-3 antagonist is an inhibitory peptide or an anti-14-3-3 antibody. The 14-3-3 antagonists are also formulated in a pharmaceutical composition and used in a method for reducing matrix metalloprotease (MMP) expression in the synovial fluid of a patient, wherein the MMP is MMP-1 or MMP-3.

The invention discloses an angiotensin-converting enzyme inhibitory peptide, and a preparation method and an application thereof, wherein the amino acid sequence of the inhibitory peptide is Leu-Ala-Ser-Pro-Thr-Met. The angiotensin-converting enzyme inhibitory peptide is prepared by tracking, screening and estimating an active ingredient for inhibiting the angiotensin-converting enzyme in mactra veneriformis by virtue of modern biochemical technical means, and purifying the active ingredient by methods of enzymolysis, ultrafiltration, reversed-phase high-performance liquid chromatography and the like; and experiment results indicate that the inhibitory peptide has an excellent effect of inhibiting the angiotensin-converting enzyme and a good anti-hypertension effect, and is good in safety performance, and thus has a bright application prospect.

The invention provides a method for preparing ACE (Angiotensin Converting Enzyme) inhibitory peptides through bean pulp enzymolysis. The method comprises the following steps that (1) high-temperature bean pulp is crushed and sieved, obtained bean pulp powder and water are mixed according to a mass ratio of 1:(4-6), the pH value is regulated to 8 to 10, and a bean pulp mixture is obtained; (2) the pH value of the bean pulp mixture is regulated to 7 to 9, a complex enzyme preparation is added, the mixture is uniformly mixed, hydrolysis is carried out for 5 to 8 hours at the temperature being 35 to 50 DEG C, after the hydrolysis is completed, hydrolysis liquid is boiled in a boiling water bath for enzyme deactivation, and mixed liquid is obtained; (3) the pH value of the mixed liquid is regulated to 6.5 to 7.5, supernatant is taken, ultrafiltration treatment is performed through an ultrafiltration membrane, and filtered liquid is obtained; and (4) the filtered liquid is subjected to vacuum freezing drying, and the ACE inhibitory peptide powder is obtained. The method for preparing ACE inhibitory peptides through bean pulp enzymolysis has the advantages that the process is simple and is easy to implement; in the whole process, the reaction conditions are mild; the compounded complex enzyme preparation is used; and the industrial processing operation is convenient.

The invention mainly relates to Larimichthys crocea connetin source ACE inhibitory peptide sequences and applications thereof. The two kinds of peptide sequences respectively are WAR and WQR, and establish a basis for prevention and treatment of hypertension. Different on-line databases are used, and after multiple times of screening, the inhibitory peptides with high efficient ACE inhibition activity are obtained. WAR and WQR are artificially synthesized, in order to verify external ACE inhibition activity of the peptides by using a high performance liquid chromatography method. The inventionrelates to two kinds of active peptides with good external ACE inhibition activity. The two kinds of peptide sequences are used for developing health food with blood pressure adjusting effects, and the purpose for prevention, control, alleviation and auxiliary treatment of hypertension is realized by long-term usage.

The invention relates to an extraction method of bean dreg protein and a method used for preparing DPP-IV inhibitory peptide with the bean dreg protein. The extraction method comprises the following steps: placing bean dreg suspension mixed by fresh bean dregs and water at the temperature of 30-50 DEG C, taking out the bean dreg suspension when pH is 3.0-5.0, collecting the lowermost layer of bean dreg protein after the suspension is layered, airing the bean dreg protein at room temperature, adding protease to prepare DPP-IV inhibitory peptide crude product powder, and then carrying out membrane separation or column chromatography to further purify to obtain DPP-IV inhibitory peptide pure product. The extraction method of the bean dreg protein is simple, no acid liquor or alkali liquor needs to be added in the preparation process, and pollution on the environment is avoided. For the method for preparing the DPP-IV inhibitory peptide with the bean dreg protein, the process is simple, the cost is low, the inhibitory ratio of the prepared DPP-IV inhibitory peptide is between 4.1% and 93.2%, and the median inhibitory concentration is between 42.70 mug/mL and 2593.64 mug/mL.

The invention discloses a method for preparing angiotensin-I-converting enzyme (ACE) inhibitory peptide by using enzymolysis goat milk casein. The method comprises the following steps of: centrifugally degreasing recovered goat milk to obtain skimmed milk; preparing casein by using an isoelectric precipitation method; freezing and drying casein precipitate; dissolving the obtained casein freeze-dried powder to prepare a casein solution; performing hydrolysis on the casein solution by adding different kinds of enzymes; and optimizing the hydrolysis condition and treating a hydrolysis process in an ultrasonic wave mode, so that catalytic activity is improved to ensure that the hydrolysis reaction is complete; and because of the obtained micromolecule ACE inhibitory peptide, obvious pressure reduction function on hypertensive can be achieved, the influence on normal blood pressure is avoided, and the method has the characteristics of no toxic and side effects, high security and easiness for absorption.