233 results about "Inhibitory peptide" patented technology

The invention discloses a xanthine oxidase inhibitory peptide with a kidney improving function and application thereof, and belongs to the technical field of biological medicines.The xanthine oxidase inhibitory peptide is screened out by conducting enzymolysis, separation and purification on litopenaeus vannamei processing by-products and utilizing a molecular docking technology, the amino acid sequence of the xanthine oxidase inhibitory peptide is Pro-Leu-Gly-Pro-Pro-Pro, and the amino acid sequence of the xanthine oxidase inhibitory peptide is Pro-Leu-Gly-Pro-Pro-Pro. And the half inhibition concentration of the polypeptide is 2.356 + / -0.2448 mM. The xanthine oxidase inhibitory peptide is proved to have an improvement effect on hyperuricemia mice, the improvement effect is mainly characterized by reducing the content of serum uric acid, creatinine and urea nitrogen of the hyperuricemia mice, inhibiting the activity of xanthine oxidase (XOD) in serum and livers of the mice, inhibiting synthesis of uric acid and improving kidney injury of the mice, and Toxinpred prediction shows that the xanthine oxidase inhibitory peptide has the effect of inhibiting the activity of xanthine oxidase (XOD) in the serum and livers of the mice. The xanthine oxidase inhibitory peptide is free of toxic and side effects, so that the xanthine oxidase inhibitory peptide has a wide application prospect in preparation of food or drugs for improving renal functions.

The invention belongs to the field of skin care products, and particularly relates to an anti-wrinkle and anti-aging composition as well as a preparation method and application thereof, and the anti-wrinkle and anti-aging composition comprises neurotransmitter inhibition peptide, signal peptide, madecassoside, inositol and glycosylglycerol. The neurotransmitter inhibition type peptide is at least three of acetyl hexapeptide-8, arginine / lysine polypeptide, dipeptide diaminobutyrylbenzylamide diacetate and acetyl octapeptide-3, and the signal type peptide is at least two of palmitoyl pentapeptide-4, decapeptide-4 and acetyl tetrapeptide-9. Compared with the prior art, all the components of the anti-wrinkle and anti-aging composition act on different anti-aging pathways and can be matched with one another from multiple aspects of oxidation resistance, inflammation resistance, moisturizing, cell viability enhancement, wrinkle reduction and the like, a more comprehensive and better anti-aging effect is provided, skin aging is comprehensively resisted, the skin is in a more young state, and the anti-wrinkle and anti-aging composition has the advantages that the anti-wrinkle and anti-aging effects are achieved. And the anti-wrinkle and anti-aging composition is small in irritation and good in stability.

An α-amylase inhibitory peptide. The peptide comprises amino acid sequences of eight adjacent amino acids X1, X2, X3, X4, X5, X6, X7, and X8, wherein each amino acid of the peptide is independently selected from a D-amino acid or an L-amino acid, and at least one of X2, X4, and X6 is W. The peptide has α-amylase inhibitory activity, has the effects of losing weight and lowering blood sugar, and can be used for preparing α-amylase inhibitors, weight-losing drugs, hypoglycemic drugs, or foods, health-care products or drugs for preventing or treating obesity-related diseases.

The invention relates to the technical field of biology, in particular to a DPP-IV inhibitory peptide extracted from buffalo cheese protein hydrolysate and application of the DPP-IV inhibitory peptide. An active component with the molecular weight smaller than 3 kDa is obtained through alkaline protease enzymolysis, ultrafiltration separation and LC-MS / MS identification, and the DPP-IV enzyme inhibitory activity IC50 value of the active component is 12.6 mg / mL. Four new DPP-IV inhibitory peptide fragments are found, are amino acid sequences in a sequence table SEQ ID NO: 1-4, have good DPP-IV inhibitory activity, and have good application prospects in being developed into functional foods or medicines for regulating blood sugar. In conclusion, the enzymolysis product and the peptide fragment can be prepared into antidiabetic drugs or functional foods, and have the advantages of being natural, safe and efficient. The invention provides a new strategy for high-valued utilization of buffalo milk resources and treatment of type 2 diabetes.

The invention discloses a tyrosinase inhibitory peptide from kelp as well as a preparation method and application of the tyrosinase inhibitory peptide. The preparation method comprises the following steps: pretreating kelp, fermenting the kelp by using lactobacillus plantarum, carrying out centrifugation, ultrafiltration and component identification on the obtained fermentation liquor to obtain the composition of kelp polypeptide, screening the tyrosinase inhibitory peptide through molecular docking, and finally carrying out solid-phase synthesis to obtain the tyrosinase inhibitory peptide prepared by the invention. The lactobacillus plantarum fermentation technology is simple and feasible, the production cost is low, equipment is easy to obtain, active ingredients in kelp can be released to the maximum extent, and the prepared polypeptide has the effect of inhibiting the activity of tyrosinase and can be used for developing a tyrosinase inhibitor.

The invention relates to a preparation method and application of yolk polypeptide with ACE inhibitory activity, and the method comprises the following steps: Q1, adding degreased yolk powder into a proper amount of water, dissolving, and adjusting the pH value to 6-8; and Q2, adding alkaline protease or flavourzyme to carry out enzymolysis for 1.5-2.5 hours under the conditions that the temperature is 50-60 DEG C and the pH value is 7-8, and then carrying out enzyme deactivation to obtain the egg yolk hydrolysate. The ACE inhibitor with high activity is prepared by adopting step-by-step enzyme hydrolysis, five ACE inhibitory peptides (KFIPL, KFLPGY, KFLPTF, APTFGKL and KLPDMILY) with high activity are screened and identified by utilizing a bioinformatics method, and in order to solve the problem that the polypeptide is unstable after being sterilized in the functional beverage, CMC and GG are used as stabilizers, so that the utilization problem of the enzymolysis polypeptide in the functional beverage is solved.

The invention discloses lactobacillus helveticus for producing DPP-IV (dipeptidyl peptidase-IV) inhibitory peptide and hypoglycemic goat milk and a preparation method thereof, goat milk is used as a raw material, and lactobacillus helveticus KD12 for producing the DPP-IV inhibitory peptide is used for fermenting the goat milk to obtain hypoglycemic lactobacillus fermented goat milk containing the DPP-IV inhibitory peptide. And drying the fermented goat milk to obtain the hypoglycemic lactic acid bacteria fermented goat milk powder containing the DPP-IV inhibitory peptide. Lactic acid bacteria of the hypoglycemic lactic acid bacteria fermented goat milk are inactivated to obtain hypoglycemic post-prebiotics goat milk, and the hypoglycemic post-prebiotics goat milk powder is obtained after the hypoglycemic post-prebiotics goat milk is concentrated and dried. The hypoglycemic goat dairy product provided by the invention has a relatively high DPP-IV inhibition rate, and can be used for inhibiting DPP-IV activity after consumers eat the hypoglycemic goat dairy product so as to reduce blood sugar and reduce the dosage of hypoglycemic drugs, so that side effects caused by the hypoglycemic drugs are reduced.

The invention belongs to the technical field of biological small molecule active peptides, and more specifically relates to a uric acid reducing active peptide, a preparation method and an application thereof. The uric acid reducing activity LQKW has remarkable XOD inhibitory activity, IC50 is 2.70 mg / mL, and the IC50 is superior to that of many known natural source XOD inhibitory peptides; good gastrointestinal digestion stability is shown, and the activity retention rate after in-vitro simulated gastrointestinal digestion is (61.84 + / -0.82)%. According to the invention, a specific binding mechanism of uric acid reduction activity and XOD active sites (Ile648, Phe649 and the like) is clarified through molecular docking, and a basis is provided for rational design based on a structure. According to the invention, the method for efficiently preparing the active peptide fragment from the white spirit vinasse is established, and the high-valued utilization of the wine brewing byproducts is realized. The uric acid reducing activity LQKW provided by the invention can be prepared through solid-phase synthesis, the process is mature, the quality is controllable, and a foundation is laid for industrialization. In addition, as the XOD inhibitor of a natural source, the uric acid reducing activity LQKW has good safety.

The invention discloses a scallop skirt ACE inhibitory peptide activity method and system based on deep learning, and relates to the technical field of bioengineering.The scallop skirt ACE inhibitory peptide activity method comprises the steps that a comprehensive data set is obtained based on simulated in-vivo test data and peptide level feature data of different peptides, key features are screened, and a training set and a test set are divided; initializing a random forest model, an SVM model and a logistic regression model, performing independent training by using the training set, and determining an optimal prediction model of the peptide antihypertensive activity based on a prediction result of the test set; extracting importance data of key features based on the optimal prediction model for the antihypertensive activity of the peptide, sorting the importance data, and visually analyzing the antihypertensive activity features, feature importance sorting and model performance of different peptides; and all key results in the analysis process are integrated and systematically stored. According to the method, normal form reference with prediction accuracy and mechanism depth can be provided for clinical transformation of marine bioactive peptides, and AI-driven novel peptide drug research and development are promoted to enter a new stage.

The present invention relates to the field of protein engineering, and specifically relates to a Morchella esculenta peptide and the use thereof. By means of comprehensively applying bioinformatic methods such as virtual enzymolysis, activity prediction, physicochemical property and safety evaluation, and molecular docking, one Morchella esculenta peptide having the potential effects of "inhibiting oxidation + skin whitening" is screened from Morchella esculenta, which peptide has a sequence of WWVCAK. In-vitro chemical experiments verify that WWVCAK is the most effective antioxidant and tyrosinase-inhibitory peptide. Therefore, WWVCAK can exert the effects of inhibting oxidation and skin whitening via multiple targets, multiple functions and multiple pathways. WWVCAK is expected to be developed and used in cosmetics as a functional skin-care ingredient with the twin effects of "inhibiting oxidation + skin whitening".

The invention discloses a mulberry leaf antihypertensive active peptide as well as a preparation method and application thereof. According to the method, mulberry leaves are used as raw materials to prepare mulberry leaf albumin, enzymolysis parameters of enzymolysis time, pH, enzyme-substrate ratio and substrate concentration are optimized through a single factor experiment and an orthogonal experiment, and optimal enzymolysis conditions for preparing the ACE inhibitory peptide crude product are provided; the high-activity ACE inhibitory peptide is identified through further purification, polypeptide sequence determination and virtual screening, the ACE inhibitory peptide has extremely high solubility and good ACE inhibitory activity, and the IC50 values of the two peptides VPSCFDLTGK and RLPDFHGL with the highest activity are 8.23 [mu] mol / L (8.765 [mu] g / mL) and 23.01 [mu] mol / L (23.58 [mu] g / mL) respectively. The active peptide can be used as an angiotensin converting enzyme inhibitory peptide, and achieves the purpose of reducing blood pressure by inhibiting ACE activity.

This invention discloses the XO-inhibiting peptide GDEY and its applications, belonging to the field of bioactive peptide technology. The amino acid sequence of the XO-inhibiting peptide GDEY is shown in SEQ ID NO.2. The invention also discloses the application of the XO-inhibiting peptide GDEY in the preparation of xanthine oxidase inhibitors and in the preparation of drugs with the effect of inhibiting uric acid levels. This invention used molecular docking and BLAST+ software to virtually screen 15 potential XO-inhibiting peptides from the complete protein sequence of Litopenaeus vannamei. High-performance liquid chromatography (HPLC) was used to determine the XO-inhibiting activity, and the results showed that 7 small molecule peptides exhibited significant XO-inhibiting activity, possessing potential value in preventing hyperuricemia.

The application discloses a polypeptide-based anti-fouling electrochemical sensor and a construction method and application thereof. In the application, cysteine is used as an anchoring end, an alpha-helix structure is formed by inserting polyproline to give a supporting effect to the whole peptide, then angiotensin converting enzyme inhibitory peptide (KSRE) and alpha-glucosidase inhibitory peptide (EKDER) are used as branches to prepare the anti-fouling polypeptide. The anti-fouling polypeptide has a better anti-fouling effect than other anti-fouling polypeptides, and the working electrode is modified by the anti-fouling polypeptide to prepare an anti-fouling electrochemical aptamer sensor for detecting AFB1, so that the anti-pollutant interference effect of the sensor can be greatly improved, the accuracy and sensitivity of AFB1 detection can be improved, and the anti-fouling electrochemical aptamer sensor has a wide application prospect.

The application discloses a Vibrio parahaemolyticus quorum sensing inhibiting peptide and application thereof, and belongs to the field of bioactive peptides. The inhibiting peptide comprises the following amino acid sequence: Ser-Phe; the application further discloses application of the quorum sensing inhibiting peptide in inhibiting Vibrio parahaemolyticus or preparing antibacterial drugs for inhibiting Vibrio parahaemolyticus. The application adopts a molecular docking technology to screen an active peptide having an inhibiting effect on a Vibrio parahaemolyticus LuxS / AI-2 quorum sensing system, ADMET property prediction is carried out on a peptide segment with better binding force, and finally, a bioactive peptide SF stably combined with LuxP, LuxQ and LuxS is obtained; the dipeptide has good in-vitro inhibiting activity on the Vibrio parahaemolyticus LuxS / AI-2 quorum sensing, and has no cytotoxicity. The dipeptide obtained by the application can be used for guiding development of a new type of antibacterial preparation applied to food, medicine and agriculture and other fields, and has great significance for human health and agricultural development.

The present disclosure relates to improved GLP-1 receptor agonist polypeptides and molecules comprising these improved GLP-1 receptor agonist polypeptides, such as molecules comprising one or more GLP-1 receptor agonist polypeptides conjugated to an anti- gastric inhibitory peptide receptor (GIPR) antibody. The present disclosure is also directed to the use of these improved GLP-1 receptor agonist polypeptides and conjugate molecules comprising these polypeptides for treating or preventing obesity, an obesity related condition, type 2 diabetes, and / or a type 2 diabetes related condition.

The invention discloses goat milk with hypoglycemic activity and a preparation method thereof, and belongs to the technical field of enzyme engineering. The goat milk is used as a raw material, enzymolysis goat milk with alpha-G inhibitory activity is obtained through compound protease hydrolysis, it is found that the enzymolysis goat milk has hypoglycemic activity, and the goat milk powder with the hypoglycemic activity is further prepared through spray drying. The alpha-G inhibitory peptides in the enzymolysis goat milk are separated and identified, 20 alpha-G inhibitory peptides are found from components with the highest alpha-G inhibition rate, the molecular weight of the alpha-G inhibitory peptides is 377-962 Da, and the alpha-G inhibitory peptides are mainly derived from beta-casein, alpha S1-casein, alpha S2-casein, kappa-casein, beta-lactoglobulin, lactoglobulin and osteopontin of the goat milk. The alpha-G inhibitory peptide is prepared by hydrolyzing the goat milk through the compound enzyme, the amino acid sequence of the alpha-G inhibitory peptide is separated and identified, the goat milk with hypoglycemic activity is developed, and theoretical basis and technical support are provided for subsequent development of hypoglycemic dairy products.

The invention discloses a walnut-derived xanthine oxidase inhibitory peptide and application thereof, and belongs to the technical field of bioactive peptide biology. The amino acid sequence of the xanthine oxidase inhibitory peptide provided by the invention is as shown in SEQ ID No. 1. Through in-vitro activity determination, the IC50 value of the inhibitory peptide is 3.34 mg / mL, and it is proved that the inhibitory peptide has high inhibitory activity on xanthine oxidase. Besides, the inhibitory peptide can reduce the levels of creatinine, urea nitrogen, adenosine deaminase, glutamic oxalacetic transaminase and glutamic-pyruvic transaminase, regulate the expression of kidney uric acid resorption protein URAT1, uric acid excretion protein GLUT9 and ABCG2, and significantly reduce the generation of uric acid, can be used for inhibiting xanthine oxidase and preventing or improving hyperuricemia, is applied to preparation of drugs for improving hyperuricemia, and has broad application prospects. The medicine takes the active peptide as the only active ingredient or one of the active ingredients, and has a good application prospect.

The invention relates to synthetic peptides of no more than 20 amino acids in size useful in the treatment of cancer.

The application belongs to the technical field of biotechnology, and particularly relates to application of albumin polypeptide gel beads in a product for treating or preventing sarcopenia. Egg white protein is used as raw material to extract protein, and albumin dipeptide-based peptidase-IV inhibitory peptide is prepared through a biological enzymolysis method. Bioinformatics analysis is used to screen out the inhibitory peptide TPYMFP, and the IC50 value of the inhibitory peptide TPYMFP for dipeptide-based peptidase-IV reaches 3.12 ± 0.49 mmol / L. Further, the optimal preparation conditions of sodium alginate SA and carboxymethyl chitosan CMCS-based gel beads CMCS / SA / TPYMFP are explored. When the SA concentration is 1.5% (w / v), the CMCS concentration is 0.5% (w / v), and the CaCl2 concentration is 1% (w / v), the polypeptide encapsulation rate is increased to 98.26% ± 0.25%. It is verified that the albumin polypeptide gel beads have good pH response characteristics, and efficient protection and intestinal target delivery of the sarcopenia inhibitory peptide are realized. The albumin polypeptide gel beads are applied to preparation of a product for treating or preventing sarcopenia, or in preparation of a related product for increasing muscle mass and strength.

The invention discloses an ACE (angiotensin converting enzyme) inhibitory peptide with antihypertensive activity and application thereof, and belongs to the technical field of active peptide biology, amino acid sequences of the ACE inhibitory peptide are EYPVK and SYPVK, the two peptides are obtained through module replacement design, the ACE inhibitory activity of the two peptides is remarkably improved compared with that of an original peptide LYPVK, IC50 values are respectively reduced to 14.82 + / -0.82 mu M and 12.83 + / -0.79 mu M from 117.14 + / -1.40 mu M, and the inhibitory activity is improved by 13.5% and 25.1%. Molecular simulation analysis shows that the interaction force between the two and ACE is stronger, and a potential modular effect exists between sequences. Besides, the polypeptide has remarkable blood pressure lowering activity on human umbilical vein endothelial cells, plays a role by regulating release of NO and ET-1, has the activity superior to that of original peptides, has the advantages of good digestive enzyme stability, small molecular weight and good water solubility, and is suitable for developing related products for lowering blood pressure.

The application discloses a flagellum inhibiting peptide of pseudomonas aeruginosa and a preparation method and application thereof, and the sequence of the flagellum inhibiting peptide is Lys-Ile-Gly-Leu-Phe-Arg-Trp-Arg. The synthetic inhibiting peptide has a time-dependent self-assembly ability, can gradually evolve from scattered granular into filamentous structure, and finally forms a stable net-like morphology. The synthetic inhibiting peptide can significantly inhibit the flagellum motility of PAO1 and other strains of pseudomonas aeruginosa, and has synergistic antibacterial activity when combined with allicin, ciprofloxacin, meropenem, levofloxacin, polymyxin B and the like. Moreover, the synthetic inhibiting peptide has obvious bacteriostatic and healing-promoting effects on burn wound infection.

The present application relates to the technical field of biology, and particularly relates to an antioxidant peptide and ACE inhibitory peptide from tuna, and a preparation method and application thereof. The amino acid sequence of the polypeptide provided by the present application is shown as SEQ ID NO. 1-6. The present application takes tuna skin waste as raw material, obtains tuna skin collagen through enzymolysis, then performs liquid chromatography-tandem mass spectrometry identification and molecular docking screening on the tuna skin collagen enzymolysis product, and obtains polypeptides with antioxidant activity and polypeptides effectively inhibiting ACE activity. The method simplifies the protein extraction step. Meanwhile, the method can improve the deep processing level of the tuna industry, achieve high-value utilization, and reduce the environmental pressure on processing waste.

The application discloses wrinkle abalone visceral-derived antioxidant peptides and ACE inhibiting peptides, and a preparation method and application thereof. 50 With DPPH free radical scavenging activity and ACE inhibiting activity as the guidance, the enzymatic hydrolysate is separated and purified through a series of methods such as ultrafiltration, dextran gel chromatography and high performance liquid chromatography, and is combined with bioinformatics screening to obtain one DPPH free radical scavenging activity peptide and three ACE inhibiting peptides, the amino acid sequences of which are shown as SEQ ID NO. 1-4, and the IC 50 values are 3.05 mg / mL, 77.43 μM, 143.93 μM and 124.10 μM respectively, and the four polypeptides have great application value. The application realizes high-value utilization of abalone viscera, and provides a reliable basis for application of abalone by-products.

The invention relates to the technical field of polypeptide synthesis, discloses a semaglutide large-fragment coupling process based on an SPPS-LPPS mixing method, and aims to solve the problems that an SPPS fragment is easy to fold and the LPPS coupling efficiency is low when semaglutide is synthesized by an existing SPPS-LPPS mixing method. SPPS is adopted for solid-phase synthesis of a semaglutide 1-21 site fragment I and a semaglutide 22-31 site fragment II, and the fragment quality is guaranteed through optimization of a solid-phase carrier, staged conformation washing and differential activation; according to the method, peptide chain folding and activating agent hydrolysis can be inhibited, the coupling efficiency and the fragment utilization rate can be improved, the purity of a coupling intermediate can be guaranteed, meanwhile, the process stability and economical efficiency can be enhanced, and the industrial production requirements of semaglutide can be met.

The present invention provides a novel gene-therapeutic agent for neurodegenerative diseases. The present invention allows AB variants to be secreted out of cells and continuously supplies tau inhibitor peptides in the cells to allow wt Aβ polymerization and wt tau polymerization to be slowed or inhibited and cytotoxicity to be reduced in the human body, and thus exhibits excellent effects of preventing, alleviating, and treating neurodegenerative diseases.

The invention belongs to the technical field of biological medicines and bioactive peptides, and relates to a xanthine oxidase inhibitory peptide derived from goat milk protein and application thereof. The amino acid sequence of the xanthine oxidase inhibitory peptide is as shown in SEQ ID NO. 1. The xanthine oxidase inhibitory peptide can be used for preparing a product for inhibiting xanthine oxidase or a product for regulating and controlling the uric acid level in a human body. The XOD regulation active peptide provided by the invention is safe in source and clear in structure, can be applied to the field of functional food or nutrition intervention, and provides a safe and natural active substance basis for diet regulation of hyperuricemia and related metabolic diseases.

The invention relates to a preparation method of a rice bran protein ACE inhibitory peptide, and belongs to the technical field of bioactive peptide preparation. The preparation method comprises the following steps: extracting rice bran protein from defatted rice bran, carrying out step-by-step enzymolysis by using alkaline protease and papain to obtain a rice bran protein ACE crude peptide solution, centrifuging, carrying out ultrafiltration by using a 3kDa ultrafiltration tube, and purifying by using gel chromatography to obtain the rice bran protein ACE inhibitory peptide. The process is simple and efficient, the cost is controllable, the obtained ACE inhibitory peptide not only has high ACE inhibitory activity, but also has high oxidation resistance, is rich in various bioactive amino acids, can be used for efficiently preparing active peptide with strong antihypertensive potential, and provides an ideal raw material for developing novel antihypertensive food, medicine and health care products.

The present application provides a tumor inhibiting peptide, which is a fragment of the N-terminal of endostatin with 45 amino acid residues or less, and contains at least the first to 20th amino acid residues of the N-terminal, and wherein the second and 18th amino acid residues of the N-terminal of endostatin are as shown herein, and optionally, there are mutations as shown herein in the 17th, 20th to 22nd positions. The present application also relates to a coding sequence of the peptide, an expression vector containing the coding sequence, a pharmaceutical composition containing the peptide, and the use of the peptide and the pharmaceutical composition in the preparation of a medicament for inhibiting, preventing or treating tumors.

The invention relates to the technical field related to microcapsules, in particular to a preparation method of a wheat alpha-glucosidase inhibitory peptide microcapsule, which comprises the following steps: by taking wheat vital gluten as a raw material, carrying out enzymolysis by alkaline protease to obtain alpha-glucosidase inhibitory peptide, and then carrying out enzymolysis by adopting a sodium alginate-chitosan composite wall material system to obtain the wheat alpha-glucosidase inhibitory peptide microcapsule. By optimizing key parameters such as the core-wall ratio of 1: 2.632, the calcium chloride concentration of 2.48% and the curing time of 31.83 min, the double-layer microcapsule with the pH response characteristic is prepared by an ionic gel method. The embedding rate of the prepared microcapsule reaches 78.26%, the 2-hour release rate in simulated gastric juice (pH 2.0) is smaller than or equal to 21.38%, the 4-hour accumulative release rate in simulated intestinal juice is larger than or equal to 84.98%, and stomach protection and intestinal targeted release of the active peptide are achieved; meanwhile, the peptide loss rate of the product under the storage condition of 4 DEG C is less than or equal to 11.13%, the loss rate in the environment with the pH value of 2.0 is only 12.72%, and the stability of the active peptide is remarkably improved. The obtained product can effectively protect the activity of the alpha-glucosidase inhibitory peptide and improve the bioavailability of the alpha-glucosidase inhibitory peptide, and a new scheme is provided for developing functional hypoglycemic food.

Disclosed herein is a series of helical sulfono-γ-AApeptides that mimic the binding mode of the α-helical HD2 domain of B-Cell Lymphoma 9 (BCL9). As disclosed herein, sulfono-γ-AApeptides can structurally and functionally mimic the α-helical domain of BCL9, and selectively disrupt β-catenin / BCL9 PPIs with even higher potency. More intriguingly, these sulfono-γ-AApeptides can enter cancer cells, bind with β-catenin and disrupt β-catenin / BCL PPI, and exhibit excellent cellular activity, which is much more potent than the BCL9 peptide. Furthermore, enzymatic stability studies demonstrated the remarkable stability of the helical sulfono-γ-AApeptides, with no degradation in the presence of pronase for 24 h, augmenting their biological potential.