Proteins & Peptides Stability and Thermal Denaturation Analysis

Proteins or peptides will undergo thermal denaturation and unfolding at too high a temperature. The melting temperature (T_m) of a protein is an important indicator of its thermal stability. As an expert in the field of proteins and peptides, CD Formulation provides a variety of protein and peptide thermal denaturation analysis services to customers around the world. Our professional team uses a series of advanced technologies to perform thermodynamic analysis on protein and peptide samples, determine their T_m, and provide professional advice on the interaction between protein and peptide drugs and ligands, formulations or excipients, and the screening of buffer stability conditions for protein drugs.

Why Conduct Protein/peptide Thermal (T_m) Stability Analysis?

Thermal stability analysis of proteins/peptides refers to the structural stability and thermal denaturation of proteins/peptides at different temperatures. It provides valuable information about the stability and structural integrity of proteins and peptides under different temperature conditions. This information is essential for many applications in biotechnology, drug development, and protein engineering.

By studying the structural changes of proteins/peptides under different temperature conditions, researchers can:

• Understand their thermal stability properties and functional performance under thermal conditions.
• Optimize purification and storage conditions.
• Evaluate the effects of mutations or modifications on stability.
• Predict the behavior of proteins/peptides under various environmental conditions.
• In-depth understanding of the folding and unfolding mechanisms of proteins.

Explore Our Protein & Peptide Stability and Thermal Denaturation Analysis Services

As a provider of protein/peptide thermal stability analysis services, CD Formulation uses a range of analytical techniques, such as differential scanning calorimetry (DSC), circular dichroism (CD), and differential scanning fluorimetry (DSF), to evaluate the thermal stability of proteins/peptides, providing key data on the stability of protein/peptide drugs. These data can be used to optimize formulations and design optimal conditions for storage, transportation, and use.

Thanks to our in-depth understanding of protein/peptide structure, we have established a systematic protein/peptide thermal stability analysis platform, which is equipped with first-class equipment and analytical techniques, including:

Thermal Shift assay (TSA)

TSA is also called differential scanning fluorimetry (DSF), a method for observing changes in protein fluorescence or absorbance when fluorescent or ultraviolet absorbing dyes bind to proteins. The specific principle is that in the natural state of proteins, hydrophobic groups are hidden inside the structure. When the temperature rises, the protein will be converted into a denatured state, exposing the hydrophobic groups. The exposed hydrophobic groups can bind to the fluorescent dye Sypro Orange and be excited to fluoresce.

• Our scientists reflect the thermal stability of protein/peptide by detecting fluorescence intensity. At different temperatures, the intensity of fluorescence is different due to the different amounts of hydrophobic groups exposed by proteins, and a fluorescence-temperature curve can be drawn.
• When the ligand binds to the protein, the stability of the protein increases, resulting in a decrease in the exposed hydrophobic groups at the same temperature. Our scientists set a higher temperature to allow the protein to fully expose the hydrophobic groups. This operation causes the fluorescence-temperature curve to shift to the right. The following figure is our workflow of a thermal shift assay.

Fig.1 Workflow of a thermal shift assay. (CD Formulation)

Differential Scanning Calorimetry (DSC)

DSC is a technique used to examine the change in heat capacity of a protein sample with temperature. It studies the thermodynamic changes that occur in a sample when the temperature changes by measuring the change in heat capacity of the sample under certain programmed heating or cooling conditions.

Our DSC analysis service can help determine parameters such as the melting temperature (Tm) and heat capacity change (ΔCp) of a protein, thereby providing information about the thermodynamic properties and thermal stability of the protein. Through the analysis of these parameters, the stability of the protein under different conditions can be evaluated, which helps to optimize the preservation, preparation, and storage conditions of the protein.

Circular Dichroism (CD) Spectroscopy

CD spectroscopy is a spectroscopic technique used to study protein structure and conformation. It can provide important information about the secondary structure (such as α helix, β fold, random coil, etc.) and thermal stability of proteins. This technique relies on monitoring the changes in the secondary structure of proteins at different temperatures to determine the thermal stability of proteins and infer Tm values.

Our scientists use CD spectroscopy to measure the absorbance values of protein/peptide at different temperatures and can obtain CD signals that change with temperature, thereby determining the thermal denaturation of proteins and their transition temperatures. This helps to understand the dynamic structural changes of proteins under heat stress conditions and provides an important reference for their stability and functional evaluation.

Fourier Transform Infrared (FTIR) Spectroscopy

FTIR spectroscopy is a non-destructive and sensitive method for studying protein/peptide structure and is used in various fields such as biotechnology, biochemistry, and pharmaceuticals. It provides valuable information about the stability of proteins under different conditions, making it an important tool for protein/peptide research.

Our scientists determine the Tm by subjecting proteins/peptides to different temperatures and monitoring their FTIR spectra to obtain information about changes in the secondary structure of proteins/peptides, such as protein unfolding and aggregation. This helps us understand the thermal stability of proteins and how different conditions affect their structure.

Why Choose Us for Protein & Peptide Stability and Thermal Denaturation Analysis?

• Extensive expertise in performing protein/peptide thermal stability testing.
• Experience from hundreds of successful projects.
• Our laboratories are equipped with first-class analytical equipment.
• Comprehensive and systematic protein/peptide thermal stability analysis techniques.
• In addition to protein and peptide stability and thermal denaturation analysis, we offer a range of other services, such as protein characterization, aggregation studies, and formulation development, providing a holistic approach to protein research.
• We provide flexible experimental design and testing options to meet the specific needs of any customer.
• Fast and efficient services ensure that our customers' projects are delivered on time.

Publication

CD Formulation masters the most advanced technical methods for protein/peptide thermal stability analysis and is committed to accurately evaluating protein/peptide thermal stability through comprehensive and systematic solutions. Please feel free to contact us if you are interested in our services. We will provide you with the most professional advice and support to ensure the smooth launch and implementation of your project.

How It Works

STEP 1

Submit a service request describing your specific research or development need.

STEP 2

We'll email you to provide your quote and confirm order details if applicable.

STEP 3

Execute the project with real-time communication, and deliver the final report promptly.