Veterinary Therapeutic Protein Structure Optimization

Veterinary therapeutic proteins often encounter challenges in clinical applications, such as high immunogenicity, short half-life, and instability. Protein structure optimization presents a vital solution to these issues before clinical research. BioVenic offers a comprehensive range of services for optimizing veterinary therapeutic proteins, including post-translational modifications, and custom labeling. These techniques are designed to improve protein structures, enhancing their functionality, stability, activity, and other properties to fulfill specific biological functions or boost pharmacological effects within organisms. We are dedicated to supporting our clients in the development of innovative protein-based therapies tailored to the specific needs of animal health.

Protein Structure Optimization Overview

Our expertise in protein structure optimization is pivotal in overcoming prevalent challenges faced by veterinary therapeutic proteins. Our services are designed not just to modify proteins but to transform their clinical efficacy. We utilize sophisticated methods like post-translational modifications and targeted custom labeling. These modifications are crucial for enhancing the therapeutic efficacy and stability of proteins, ensuring they perform optimally in diverse biological systems. Our tailored approach to developing protein-based therapies enables us to meet the specific needs of veterinary health, providing our clients with robust and innovative solutions to advance animal care.

Protein Post-translational Modification Service

Our services are dedicated to assisting clients in modifying veterinary therapeutic protein to improve its safety, stability, and activity. This includes employing techniques such as protein phosphorylation, acetylation, methylation, glycosylation, PEGylation, and conjugation. We provide tailored solutions to meet diverse client needs, considering factors such as various types of modifications, different proteins, target animal species, and specific research objectives. Our commitment is to deliver high-quality services that precisely cater to the unique requirements of each client.

• Protein Phosphorylation
  Protein phosphorylation is one of the most prevalent and significant modifications observed in cellular processes. Our service aims to improve the protein you provide by utilizing phosphorylation to address its shortcomings.

Fig.1 The mechanism of protein phosphorylation. ^{1, 2}

• Protein Acetylation
  Protein acetylation refers to the transfer of an acetyl group (CH₃CO) onto a protein. While the most widely studied acetylations occur on amino groups, acetylation can also happen on serine, threonine, and histidine residues. We help clients enhance the stability of therapeutic proteins by providing acetylation modification services.

Fig.2 The mechanism of protein acetylation. ^{3, 4}

• Protein Methylation
  Protein methylation involves the addition of a methyl group to a protein, which regulates its function. For example, proteins with arginine methylation participate in various cellular processes, such as RNA processing, transcription regulation, and DNA damage repair. Our service assists clients by methylating their veterinary proteins, enhancing their functionality.

Fig.3 The mechanism of protein methylation. ^{5, 6}

• Protein Glycosylation
  Glycation contributes to the heterogeneity of recombinant therapeutic proteins. Glycosylation can protect against nonspecific proteolytic degradation, reduce renal clearance through negatively charged sialic acids at glycan chain termini, and decrease kidney glomerular filtration due to the increased molecular weight and hydrodynamic radius of the glycoprotein. Our glycosylation service is used to prolong the half-life of these veterinary proteins.

Fig.4 Common glycan modifications found on proteins. ^{7, 8}

• Protein PEGylation
  Protein PEGylation is a biotechnological process where polyethylene glycol (PEG) molecules are covalently attached to therapeutic proteins. This modification service aims to improve the pharmacokinetic properties and stability of the proteins.

Fig.5 The mechanism of protein PEGylation. ^{9, 10}

• Other Protein Modification Methods.
  In addition to the methods previously mentioned, BioVenic also offers other advanced protein modification techniques, expanding the scope and impact of our services. These include protein hydroxylation, which enhances protein solubility and stability; protein ubiquitination, crucial for regulating protein degradation and signaling; protein lipidation, which improves the association of proteins with cellular membranes; and protein SUMOylation, which plays a key role in modulating protein function and localization. These specialized services significantly enhance the versatility and efficacy of our protein customization and conjugation capabilities. By providing such comprehensive and cutting-edge techniques, BioVenic caters to a broad range of preclinical research and therapeutic applications, helping clients and healthcare professionals develop more effective and targeted animal treatments.

Custom Labeling and Conjugation Service

BioVenic is a leading provider of comprehensive, high-quality recombinant protein and custom protein services, catering to a diverse array of research and therapeutic needs. Our offerings include a wide array of protein customization and conjugation options, such as fluorophores for sophisticated imaging techniques, biotin for improved binding studies, horseradish peroxidase (HRP) for enhanced enzymatic signal amplification in assays, and various carrier proteins to increase stability and improve delivery of therapeutic proteins. This conjugation process is essential for enhancing the functionality and application of proteins in various research and therapeutic contexts.

Service Workflow

BioVenic offers an integrated service for optimizing veterinary therapeutic proteins before clinical application. Please submit your inquiry along with specific requirements for protein structure optimization. We will then design the experiment and arrange a meeting to finalize the cooperation details through a contract. Once the contract is signed, our team will commence the optimization service and conduct a thorough data analysis. We will conclude our service by delivering a detailed and professional report, complete with standard protocols and results.

Fig.6 The veterinary therapeutic protein structure optimization service workflow. (BioVenic Original)

Why Choose Us?

BioVenic, harnesses advanced technologies and deep expertise in protein structure optimization to enhance the properties of therapeutic proteins, ensuring improved safety, solubility, stability, immunogenicity, and pharmacological effects. Our laboratory is equipped to meet the diverse needs of various species, from livestock and poultry to companion animals. With our customized services, we are dedicated to delivering precise solutions tailored to your specific requirements. We invite you to reach out to us with your inquiries and explore how our specialized services can benefit your veterinary applications.

References

1. Seok, Seung-Hyeon. "Structural insights into protein regulation by phosphorylation and substrate recognition of protein kinases/phosphatases." Life 11.9 (2021): 957.
2. Image retrieved from Figure 1 "The overall mechanism of protein phosphorylation regulated by protein kinases and protein phosphatase". Seok, Seung-Hyeon, 2021, used under CC BY 4.0, the title was changed to "The mechanism of protein phosphorylation".
3. Christensen, David G., et al. "Post-translational protein acetylation: an elegant mechanism for bacteria to dynamically regulate metabolic functions." Frontiers in Microbiology 10 (2019): 1604.
4. Image retrieved from Figure 1 "Mechanisms of Acetylation". Christensen, David G., et al, 2019, used under CC BY 4.0, the title was changed to "The mechanism of protein acetylation".
5. Kim, Eunji, et al. "DNA or protein methylation-dependent regulation of activator protein-1 function." Cells 10.2 (2021): 461.
6. Image retrieved from Figure 1 "The methylation processes. Methyltransferases transfer a methyl group from a methyl donor (S-adenosylmethionine [SAM]) to a substrate". Kim, Eunji, et al., 2021, used under CC BY 4.0, the title was changed to "The mechanism of protein methylation".
7. Goettig, Peter. "Effects of glycosylation on the enzymatic activity and mechanisms of proteases." International Journal of Molecular Sciences 17.12 (2016): 1969.
8. Image retrieved from "Graphical Abstract". 7. Goettig, Peter, 2016, used under CC BY 4.0, the title was changed to "Common glycan modifications found on proteins".
9. Dozier, Jonathan K., and Mark D. Distefano. "Site-specific PEGylation of therapeutic proteins." International Journal of Molecular Sciences 16.10 (2015): 25831-25864.
10. Image retrieved from Figure 1 "The general strategy for protein PEGylation". Dozier, Jonathan K., and Mark D. Distefano, 2015, used under CC BY 4.0, the title was changed to " The mechanism of protein PEGylation".