Valprotide acetate is an artificially synthetic octapeptide somatostatin drug, which is clinically used for gastrointestinal bleeding, acromegaly, pancreatitis and other diseases, and also has a certain tumor inhibitory effect on neuroendocrine tumors, prostate cancer, etc. Therefore, using valprotide acetate as a template can improve the biocompatibility of precious metal nanomaterials. Valprotide acetate was approved for marketing in 2004 with the chemical name D-phenylalanyl-cysteine-tyrodyl-D-chromatoyl-lysazyl-valinel-cysteine-tryptamide-cyclo[2-7]-disulfide monoacetate.

Basic information:
Chinese name: valprotide acetate
English name: Vapreotide
Company number: GT-B016
CAS Number: 103222-11-3
Sequence: D-Phe-[Cys-Tyr-D-Trp-Lys-Val-Cys]-Trp-NH2
Formula: C57H70N12O9S2
Molecular weight: 1131.4

Physical and chemical properties
When valprotide acetate is dissolved in an acidic aqueous solution, it has a large positive charge on the surface because it is below its isoelectric point (pI≈10.0). In addition, because it is a small molecule compound composed of amino acids, the acidic environment will change the spatial conformation of the template, mainly manifested in α-helix and β-folding, etc., so that it can maintain a stable secondary and tertiary structure in aqueous solution for a long time. Similarly, when the valproptide acetate template is heat-treated at high temperature (≥70°C), its supersecondary structure (αα, βαβ, ββ) will change significantly, and the peptide chain forms a three-structure local fold area on the basis of the secondary structure or supersecondary structure, which is a relatively independent tight sphere, that is, the domain, which will also change due to changes in the environment. Of course, there are other means of processing peptide chains, such as heavy metal salts, ultrasound, etc. After the above acid and heat treatments, valprotide acetate will form a relatively stable three-dimensional structure, and the specific groups will be regularly exposed on the surface of the template. Therefore, when the metal salt solution is co-incubated with the pretreated Peptide acetate solution, the metal ions will bind to the surface of the template under the action of electrostatic forces and specific groups, and due to biomineralization, these attached ions will be reduced into trace small crystals, which we call "crystal seeds", and then under the action of suitable reducing agents, a large number of free metal ions are continuously reduced, and grow along one or several crystal planes of the "crystal seed", and finally form nanomaterials with the expected morphology.

Application
Vapapritide acid can be used as a biological template, and its advantages include: (1) small molecular weight, simple structure, and can be analyzed and designed according to the morphology of the intended material; (2) In acidic solution, the surface of vapritide acetate will carry a large amount of positive charge, and the precursor metal ions will be continuously adsorbed to the surface of the template through electrostatic force and specific groups, thereby increasing the metal load of nanomaterials and conducive to better their physical and chemical properties. (3) Valprotide acetate belongs to the somatostatin class, which has high biocompatibility, and the precious metal nanomaterials made from it as templates can be used in the field of physical medicine. Examples of its applications are as follows:
1) Preparation of a silver-gold alloy nanospherical shell based on valproptide acetate, It is mainly prepared according to the ratio of 0.91~1.13mg vapritide acetate per ml of hydrochloric acid solution, treated at 65~67°C for 20~24min, according to the ratio of 1:3~9, silver nitrate solution is added, put into a water bath constant temperature shaker at 24°C for 24~26h, according to the ratio of silver nitrate: sodium borohydride is 1:1~2, and then the reducing agent sodium borohydride is added drop by drop, and the reaction is 16~18min at 24°C; and then placed in a boiling water bath at 100°C for 10min, and gold trichloride solution is added according to the ratio of gold trichloride:silver nitrate molar ratio of 1:25~45 , 100°C boiling water bath for 2~4min, silver-gold alloy nanospheres with particle size of 90~110nm were prepared. The present invention is easy to control, simple to operate, green and environmentally friendly, mild reaction conditions, and the prepared silver-gold alloy has uniform particle size and good dispersion.
2) Preparation of palladium nanocubes. Valprotide acetate was dissolved in a hydrochloric acid solution with a pH of 1~3, A concentration of 0.1~0.2mM was prepared into 300μL vaprotide acetate solution, and the palladium chloride solution was added to the molar ratio of vaprotide acetate:palladium chloride at a ratio of 1:20~60, and placed in a constant temperature metal bath at 60~80°C. According to the molar ratio of palladium chloride:ascorbic acid was 1:10~50, the newly prepared ascorbic acid solution was quickly added for reduction, and the solution gradually changed from light yellow to black-brown, so as to obtain palladium nanocubes with regular morphology and uniform particle size. The preparation process of the present invention is simple and easy to operate; And this method does not use toxic reagents, which is green and environmentally friendly; The prepared palladium nanocubes have regular morphology, good photothermal conversion performance, and rapid heating after short-term low-power laser irradiation, which can be used as hyperthermic agents for cancer treatment.
3) Silver nanospheres were prepared with valprotide acetate as a biological template, It is mainly formulated into a vaprotide acetate solution with a concentration of 0.2~0.4mM, kept warm at 70~80°C for 10~30min, and the silver nitrate solution is added to the vapritide acetate solution at a ratio of 1:6~8, put into a water bath constant temperature shaker, 80~100rpm, 25°C for 12~24h, according to the molar ratio of silver nitrate solution: sodium borohydride is added to the incubated solution, the drop rate is 2 drops/minute, 60μL per drop, 25°C reaction for 5~15min, so as to obtain silver nanospherical shells with uniform particle size and good dispersion of 80~100nm. The silver nanosphere shell prepared by the invention overcomes the shortcomings of easy aggregation and precipitation in the traditional preparation process, and has a high metal load.

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1. Introduction

Peptides are compounds formed by two or more amino acids linked by peptide bonds, which are widely present in living organisms and participate in a variety of physiological processes, including cell signaling, enzyme catalysis, immune response, and metabolic regulation. In recent years, with the development of biosynthesis and chemical synthesis technologies, peptide customization services have increasingly become a core tool in life sciences, pharmaceutical research and development, and molecular biology research.
The editor will introduce in detail the technical principles, main processes, quality control processes and typical applications of peptide customization in scientific research.

2. Technical principle of peptide customization

Peptide customization is the process of synthesizing amino acids in specific sequences to obtain the target peptide molecules with the desired structure and function. Its main synthesis techniques include:

1. Solid Phase Peptide Synthesis (SPPS)
   At present, a wide range of synthesis technologies are used. By fixing one amino acid on a solid-phase resin, then gradually adding other amino acids, using condensing agents (e.g., HBTU, DIC) to connect the amino acid residues, and finally chemically cutting the synthesized peptides from the solid-phase carrier.
   Advantages: high degree of automation; can synthesize long peptides; Easy to purify and modify.
2. Liquid Phase Synthesis
   It is suitable for short-chain peptides and large-scale industrial synthesis, with mild reaction conditions but cumbersome steps.

3.Detailed explanation of the customization process

A standard peptide customization process generally includes the following key steps:

1. Design and sequence confirmation
   Customers provide amino acid sequence or functional requirements;
   The service party analyzes the sequence (whether it contains special modifications, whether it contains disulfide bonds, whether it is water-soluble, etc.);
   Bioinformatics tools were used to predict secondary structure, hydrophilicity and other parameters to assist in design.
2. Synthesis stage
   Choose the appropriate solid-phase carrier (e.g., Rink amide resin, Wang resin);
   Precise control of the coupling reaction of each amino acid;
   Add protective groups (e.g., Fmoc, Boc) to avoid side effects.
3. Purification and analysis
   High Performance Liquid Chromatography (HPLC) for separation and purification, the purity can reach more than 95%;
   Molecular weight was confirmed using mass spectrometry (MALDI-TOF, ESI-MS);
   Nuclear magnetic resonance (NMR) and circular dichroism (CD) assisted analysis are performed if necessary.
4. Packaging and quality control
   Provide lyophilized powder according to customer needs;
   Evaluation of storage conditions by stability tests (high temperature, light, hydrolysis);
   Provide Quality Analysis Report (COA) and MSDS documentation.

4. Types of peptide modifications

Common functional touch-ups in the customization process include:
N-terminal modifications: acetylation, biotin, biotinylation;
C-terminal modification: amideation, esterification;
Fluorescent labeling: FITC, TAMRA;
phosphorylation/glycosylation: mimicking naturally modified peptides;
Disulfide bond bridging: stabilize the spatial structure.

5. Application of peptide customization in scientific research

1. Antibody preparation and epitope analysis
   Researchers can synthesize specific epitope peptides as antigens for the preparation of polyclonal or monoclonal antibodies.
2. Cell signaling pathway research
   Synthesis of phosphorylated or mutant site peptides for protein kinase activity screening, pathway validation, etc.
3. Pharmacological screening and functional verification
   peptide antagonists and agonist mimics;
   Combination studies with GPCR and other targets.
4. Immunology research
   Vaccine research and development, immunogenicity assessment, peptide library construction, etc.
5. Protein interaction experiments (e.g., pull-down)
   Protein function and interaction analysis are achieved by capturing protein complexes with tags (e.g., His, FLAG, Biotin) with peptides.

6. Technical challenges and development trends and Challenge:

Low synthesis efficiency of long-chain (>50aa) peptides;
Hydrophobic polypeptides are easy to aggregate and affect solubility;
The synthesis steps of special modifications (such as glycosylation) are complex and costly.
Trend:
Accelerate the promotion of intelligent and peptide synthesis automation equipment;
Peptide drug development drives breakthroughs in functional modification technology;
Custom processes are integrated with bioinformatics to improve design accuracy.

7. Summary

Peptide customization is a highly integrated biosynthesis and chemical engineering technology that requires not only precise equipment and materials, but also precise design logic and analytical capabilities. In the field of scientific research, it has become an indispensable technical support for experimental design and biological validation. With the upgrading of technology and the deepening of application, it will release greater potential in the future in basic scientific research, precision medicine, biopharmaceuticals and other directions.

Beinaglutide is a human GLP-1 polypeptide with CAS number 123475-27-4 and almost 100% homology to human GLP-1 (7-36). Benaglutide has shown dose-dependent effects in glycemic control, inhibition of food intake and gastric emptying, and promotion of weight loss. Benaglutide has the potential to study overweight/obesity and nonalcoholic steatohepatitis (NASH).

Basic information
Chinese name: Benaglutide
English name: Beinaglutide
Company number: GT-M19402
CAS Number: 123475-27-4
Sequence: HAEGTFTSDVSSYLEGQAAKEFIAWLVKGR
Formula: C149H225N39O46
Molecular weight: 3298.61

This high degree of structural similarity allows benaglutide to mimic GLP-1 in the human body, thereby acting in multiple physiological processes. First, benaglutide has shown significant results in blood sugar control. It helps regulate blood sugar levels and keeps them within a relatively stable range, which is especially important for diabetics.
In addition, benaglutide also has a significant inhibitory effect on food intake and gastric emptying. This means that when the body ingests benaglutide, it can slow down the emptying of the stomach, which can make people feel fuller, help reduce food intake, and help with weight management. In addition, benaglutide is also able to promote weight loss, which has been confirmed in several studies.

It is important to note that the effects of benaglutide are dose-dependent, i.e., its effects are enhanced with increasing doses. This allows doctors to adjust the dosage of benaglutide according to the patient's specific situation to achieve the best treatment effect.

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Amycretin, developed by Novo Nordisk, is a single-molecule long-acting GLP-1 and amylin receptor agonist. Its mechanism of action achieves weight loss by simultaneously activating both receptors: • GLP-1 receptor activation: delays gastric emptying, promotes insulin secretion, and lowers blood sugar; • Activation of amylin receptors: It directly acts on the central nervous system, inhibits appetite and reduces energy intake. In July 2025, the molecular structure of Amycretin, a GLP-1 series product under Novo Nordisk, was officially disclosed.

The amycretin structure comprises a GLP-1 receptor agonist moiety (dark blue) and an amylin receptor agonist moiety (light blue) connected by a linker region (yellow). The amycretin peptide is acylated with a C18 diacid-based sidechain (white) at position K37 (when employing GLP-1 7-37 numbering). Aib, α-aminoisobutyric acid; Ala, alanine; Arg, arginine; Asp, aspartic acid; C, carbon; Gln, glutamine; GLP-1, glucagon-like peptide-1; Glu, glutamic acid; Gly, glycine; H, hydrogen; His, histidine; Ile, isoleucine; K, lysine; Leu, leucine; Lys, lysine; N, nitrogen; O, oxygen; OH, hydroxyl group; Phe, phenylalanine; Pro, proline; Ser, serine; Thr, threonine; Trp, tryptophan; Tyr, tyrosine; Val, valine.

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The synthesis of GLP-1 impurities is difficult. Now in China domestic market, generally impurities are provided by professional CRO which focus on peptide impurities.
Anyone need to know more, plz download the impurities list below.

GLP-1 impurities.xlsx
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