Veterinary Therapeutic Protein and Peptide High Order Structure Characterization

The folding conformation and aggregation of proteins and peptides are crucial for their function, stability, and effectiveness. These all belong to the high-order structures (HOS) of proteins/peptides. BioVenic provides HOS characterization services for veterinary therapeutic proteins and peptides, offering detailed insights into protein folding and three-dimensional structures using advanced technologies.

Protein and Peptide High Order Structure Characterization Overview

Understanding the HOS of protein and peptide drugs is essential for ensuring their efficacy and safety. This involves analyzing aspects such as folding, conformation, and aggregation. BioVenic specializes in veterinary therapeutics and offers species-specific services using advanced techniques to provide comprehensive insights into these structural characteristics.

Fig.1 The high-order structure characterization of therapeutic protein and peptide. (BioVenic Original)

Protein and Peptide High Order Structure Characterization Services

• Circular Dichroism (CD)

CD (Circular Dichroism) is an analytical method used to examine the structure of chiral molecules by measuring their differential absorption of left- and right-handed circularly polarized light. BioVenic employs a CD spectrometer to analyze the secondary structure of veterinary therapeutic proteins and peptides in solution, simulating their natural physiological environment.

Fig.2 Instrumentation of CD spectroscope. ^{1, 2}

• Fourier Transform Infrared Spectroscopy (FT-IR)

FTIR spectroscopy involves measuring the infrared absorption of a sample to gain detailed insights into molecular vibrations, chemical bonds, and structures. BioVenic utilizes FTIR technology to provide services that characterize the secondary structure and conformation of veterinary therapeutic proteins and peptides, aiding in the assessment of their structural integrity and stability during the discovery and quality development stages.

Fig.3 Principles of the FT-IR. ^{3, 4}

• Hydrogen-Deuterium Exchange Mass Spectrometry (HDX MS)

Hydrogen-deuterium exchange Mass Spectrometry (HDX MS) is a sophisticated technique used to study the higher-order structures (HOS) and dynamics of proteins and peptides. BioVenic offers HDX MS services to provide clients with deep insights into the structural and conformational properties of veterinary therapeutic proteins and peptides, supporting their development and optimization.

Fig.4 Schematic diagram of the HDX-MS workflow. ^{5, 6}

• Differential Scanning Calorimetry (DSC)

Differential Scanning Calorimetry (DSC) measures the heat capacity changes associated with the thermal denaturation of biomolecules, helping to study their thermal stability and folding properties. BioVenic uses DSC technology to assess the thermal stability of veterinary therapeutic proteins and peptides, which is vital for optimizing formulations, and storage conditions, and ensuring the biological activity and efficacy of these therapeutics.

Fig.5 Schematic representation of protein stability studies using DSC. ^{7, 8}

• Nuclear Magnetic Resonance (NMR)

Nuclear Magnetic Resonance (NMR) spectroscopy is used to determine the three-dimensional structure, dynamics, and interactions of proteins and peptides at the atomic level by leveraging the magnetic properties of atomic nuclei in a magnetic field. BioVenic specializes in NMR analysis of veterinary therapeutic proteins and peptides, using advanced techniques and stable isotope labeling to elucidate functional mechanisms and potential drug targets.

Fig.6 Workflow of solid-state NMR. ^{9, 10}

• X-Ray Crystallography (XRC)

BioVenic offers services in 3D structural characterization of veterinary therapeutic proteins and peptides using X-ray crystallography. Our team is experienced in optimizing the growth of high-quality protein crystals, enabling the precise determination of atomic positions within the crystallized molecules. This detailed structural information is crucial for understanding protein functions, identifying drug target sites, and guiding drug design.

Fig.7 Workflow for molecular structure determination by XRC. (BioVenic Original)

Service Workflow

The workflow for characterizing the HOS of veterinary therapeutic proteins and peptides begins with a consultation to define project goals and design a customized plan. After finalizing and signing the contract, samples are collected and prepared for analysis. The characterization experiments are then conducted using techniques such as NMR or X-ray. Following data collection, the results are analyzed to determine structural details. The findings are compiled into a comprehensive report, which is reviewed and finalized with the client.

Fig.8 The service workflow of veterinary therapeutic protein and peptide higher-order structure analysis. (BioVenic Original)

Why Choose Us?

Due to the complexity, characterizing the high-order structure is crucial for a comprehensive understanding of the protein's stability, folding, structure, and functional activity. BioVenic offers HOS characterization services for veterinary therapeutic proteins and peptides, assisting in advancing your veterinary therapeutic protein and peptide development projects. If you require this type of service, please contact us immediately.

References

1. Pignataro, María Florencia, María Georgina Herrera, and Verónica Isabel Dodero. "Evaluation of peptide/protein self-assembly and aggregation by spectroscopic methods." Molecules 25.20 (2020): 4854.
2. Image retrieved from Figure 10 "Circular Dichroism as a tool for the study of protein secondary and tertiary structure".Pignataro, María Florencia, María Georgina Herrera, and Verónica Isabel Dodero.; 2020, used under CC BY 4.0. The original image was modified by extracting and using only part a and the title was changed to "Instrumentation of CD spectroscope".
3. Patrizi, Barbara, et al. "Dioxin and related compound detection: Perspectives for optical monitoring." International Journal of Molecular Sciences 20.11 (2019): 2671.
4. Image retrieved from Figure 2 "Principles of the Fourier-Transform Infrared Spectroscopy (FT-IR)". Patrizi, Barbara, et al.; 2019, used under CC BY 4.0, the title was changed to " Principles of the FT-IR ".
5. Narang, Dominic, et al. "HDX-MS: an analytical tool to capture protein motion in action." Biomedicines 8.7 (2020): 224.
6. Image retrieved from Figure 3 "Schematic overview of top-down and bottom-up HDX-MS workflow". Narang, Dominic, et al.; 2020, used under CC BY 4.0, the title was changed to "Schematic diagram of the HDX-MS workflow".
7. Ghandi, Khashayar. "A review of ionic liquids, their limits and applications." Green and Sustainable Chemistry 2014 (2014).
8. Image retrieved from Figure 3 "Simple schematic diagram of differential scanning calorimetry (DSC)". Ghandi, Khashayar; 2014, used under CC BY 4.0, the title was changed to "Schematic representation of protein stability studies using DSC".
9. Rankin, Naomi J., et al. "The emergence of proton nuclear magnetic resonance metabolomics in the cardiovascular arena as viewed from a clinical perspective." Atherosclerosis 237.1 (2014): 287-300.
10. Image retrieved from Figure 1 "Simplified diagram of a nuclear magnetic resonance spectrometer." Rankin, Naomi J., et al.; 2014, used under CC BY 3.0, the title was changed to "Workflow of solid-state NMR".