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Dynamic Light Scattering (DLS) Service

Q: Q3: What is the difference between DLS and other particle sizing methods?

A3: Method Strength Limitation DLS Rapid, solution-based, minimal sample prep Sensitive to large aggregates Size Exclusion Chromatography Separates species Requires longer analysis time Electron Microscopy Direct visualization Complex preparation Nanoparticle Tracking Analysis Individual particle tracking Requires optimal concentration range

Dynamic Light Scattering (DLS) Services for Biopharmaceutical Development

At Creative Proteomics, our Dynamic Light Scattering (DLS) services are strategically designed to support particle size determination, protein aggregation analysis, and antibody drug development workflows across early discovery, pre-formulation, and CMC development stages. With rich experience in biophysical characterization, we deliver high-sensitivity DLS measurements tailored to the real-world challenges faced by biomedical researchers, pharmaceutical R&D teams, and CRO collaborators.
DLS plays a central role in evaluating hydrodynamic size distributions, colloidal stability, and aggregation behavior of therapeutic proteins, monoclonal antibodies, viral vectors, and nanomedicines. Our service platform integrates DLS with static light scattering (SLS), zeta potential analysis, and orthogonal chromatographic methods to deliver robust, decision-enabling data outputs.
For clients requiring comprehensive characterization, DLS integrates seamlessly with our:

Figure 1. Scheme of a light scattering setup (Falke S, et al., 2019).

Advantages of Our DLS Services

High sensitivity to early aggregation events
Broad particle size measurement range
Minimal sample preparation
Low sample consumption
High-throughput screening capability
Temperature-controlled stability profiling

Our DLS services are fully customizable and seamlessly integrated into broader proteomics and stability testing workflows.

Protein Aggregation Analysis in Antibody Drug Development

Protein aggregation remains one of the most significant risks in antibody drug development. Even low levels of soluble aggregates can compromise stability, reduce efficacy, and complicate manufacturing.
Our DLS-based protein aggregation analysis enables:

Early detection of oligomers and pre-aggregates
Quantification of aggregate size distribution
Comparative stability profiling under stress conditions
High-throughput formulation screening

For advanced aggregate profiling, we integrate DLS with complementary techniques, such as SEC-MALS, to obtain absolute molecular weight confirmation and improve resolution in heterogeneous systems.

Advanced Particle Size Determination for Biologics

Our DLS services support size characterization across:

Monoclonal antibodies and antibody fragments
Fusion proteins and bispecific constructs
Viral vectors (AAV, lentivirus)
Lipid nanoparticles (LNPs) and liposomes
Protein-based nanocapsules
Polymer conjugates and macromolecular complexes

Protein-Protein Interaction Studies and Colloidal Stability Assessment

Beyond size measurement, DLS provides quantitative insight into intermolecular interactions that drive aggregation behavior.
We determine:

Diffusion interaction parameter (kD)
Second virial coefficient (B22)
Theoretical diffusion constant at zero concentration (D₀)

Thermal Stability and Stress-Induced Aggregation Profiling

Temperature-induced stress studies are indispensable for evaluating antibody stability and predicting long-term behavior.
Our DLS platform supports:

Temperature ramp experiments (4°C–85°C)
Determinant of aggregation onset temperature
Monitoring of Tsize and Tscattering
Thermal denaturation curve analysis

Integrated DLS Platforms

Our instrumentation supports both cuvette-based precision analysis and high-throughput plate formats (96-1536 wells), enabling:

Design-of-Experiment (DoE) formulation screening
Parallel condition comparison
Minimal sample volume (as low as 2-4 µL)

Characterization of Nanomedicines and Gene Therapy Vectors

In addition to protein therapeutics, DLS is widely applied to advanced delivery systems, including:

Lipid nanoparticles (LNPs)
Liposomes
Virus-like particles
Adeno-associated virus (AAV) preparations
Polymers-based nanocarriers

DLS provides rapid evaluation of:

Particle size distribution
Aggregate content
Particle concentration (when combined with static light scattering)
Thermal stability

Creative Proteomics' DLS Service Workflow

Sample Preparation: Controlled handling to minimize dust/particulate contamination; optimize concentration, buffer, and viscosity.
Experimental Design: Tailored measurement conditions; high-throughput plate-based screening for multiple formulations.
DLS Measurement: Laser-based detection of Brownian motion; autocorrelation analysis to calculate hydrodynamic radius.
Data Analysis: Z-average particle size, polydispersity index, intensity- and volume-weighted distributions; detect aggregates and oligomers.
Stability & Interaction Assessment: Evaluate thermal stability, aggregation onset, and protein–protein interactions; derive diffusion and interaction parameters.

Workflow of Creative Proteomics' DLS service

Sample Requirements

Sample Type	Proteins, peptides, antibodies, oligonucleotides, nanoparticles, liposomes, lipid nanoparticles, virus-like particles
Concentration Range	0.1 mg/mL – 100 mg/mL (protein samples) 10^9 – 10^12 particles/mL (nanoparticles/viral vectors)
Volume Required	2–10 µL for plate-based assays 20–100 µL for cuvette-based measurements
Buffer Conditions	Typical formulation buffers are acceptable; avoid high particulate contamination
Temperature Requirements	4°C – 85°C

Why Choose Creative Proteomics for DLS Services?

Customized method development
Integrated stability and aggregation workflows
Expert interpretation beyond raw size data
Rapid turnaround times
Comprehensive reporting tailored to regulatory and development needs

FAQ

Q1: How does Dynamic Light Scattering (DLS) measure particle size?

A1: DLS measures the size of particles in a solution by tracking their natural motion, called Brownian motion. A laser shines through the sample, and the scattered light fluctuates as particles move. These fluctuations are analyzed to calculate the particle's diffusion rate, which is then converted into a size estimate called the hydrodynamic radius. This method works for proteins, nanoparticles, and other biomolecules without requiring separation.

Q2: How does DLS detect protein–protein interactions?

A2: DLS can measure whether proteins attract or repel each other in solution. By analyzing how diffusion changes with concentration, we can quantify interaction tendencies. Proteins that stick together form larger complexes, which increase the measured particle size. This information helps optimize high-concentration formulations, such as antibody therapies.

Q3: What is the difference between DLS and other particle sizing methods?

A3:

Method	Strength	Limitation
DLS	Rapid, solution-based, minimal sample prep	Sensitive to large aggregates
Size Exclusion Chromatography	Separates species	Requires longer analysis time
Electron Microscopy	Direct visualization	Complex preparation
Nanoparticle Tracking Analysis	Individual particle tracking	Requires optimal concentration range

Q4: How does DLS complement other analytical methods?

A4: DLS is fast, non-destructive, and requires minimal sample preparation, making it ideal for early screening. For detailed structural insights or highly complex samples, techniques like size-exclusion chromatography, electron microscopy, or multi-angle light scattering can be used alongside DLS. Together, these methods provide a comprehensive view of particle size, aggregation, and stability.

Case Study

Case: Aggregation Kinetics for IgG1-Based Monoclonal Antibody Therapeutics

Authors: Singla A, et al.

Journal: The AAPS journal

Year: 2016

DOI: 10.1208/s12248-016-9887-0

Background

Monoclonal antibodies (mAbs) are widely used as therapeutic agents for diseases such as cancer, autoimmune disorders, and infectious diseases. However, protein aggregation is a major challenge in antibody drug development because it can lead to loss of biological activity, reduced product quality, and increased immunogenicity. Aggregation may occur during production, purification, formulation, or storage. Understanding the mechanisms and kinetics of aggregation under different environmental conditions is essential for improving antibody stability and manufacturing processes.

Methods

Size Exclusion Chromatography (SEC): to measure monomer loss and quantify aggregate formation.
Dynamic Light Scattering (DLS): to determine the hydrodynamic size of antibody aggregates and identify oligomer species such as monomers, dimers, trimers, tetramers, and pentamers.
Circular Dichroism (CD) spectroscopy: to analyze structural changes in the antibody's secondary structure.

Results

The study found that environmental conditions strongly influence antibody aggregation. DLS analysis confirmed the formation of multiple oligomeric species, with dimers acting as the critical nucleus for aggregation.

Key findings include:

pH: Low pH (pH 3.0) significantly increased aggregation, while higher pH values maintained stability.
Temperature: Aggregation increased with temperature, with the highest aggregation observed at 30°C.
Salt concentration: Increasing salt levels accelerated aggregation by reducing electrostatic repulsion between protein molecules.
Buffer type: Citrate buffer promoted aggregation more than acetate or glycine buffers.

Figure 2. SEC chromatograms and DLS data for oligomer distribution analysis.

Figure 3. DLS data of various aggregate species separated by SEC.

Results of monoclonal antibody aggregation

Figure 4. Aggregation of a monoclonal antibody therapeutic.

Conclusion

The study concludes that aggregation of IgG1 monoclonal antibodies is strongly influenced by environmental conditions, particularly pH, temperature, salt concentration, and buffer composition. The results indicate that aggregation follows a nucleation-driven mechanism, with dimers serving as the initial nuclei for aggregate growth.

Demo

Demo: The characterization of exosomes from fibrosarcoma cell and the useful usage of Dynamic Light Scattering (DLS) for their evaluation

This study characterizes fibrosarcoma-derived exosomes and demonstrates that dynamic light scattering (DLS) enables rapid measurement of their size and homogeneity.

Identify the average radius of exosomes by DLS

Figure 5. The average radius of exosomes derived from the WEHI-164 cell line was identified by DLS.

References

Singla A, et al. Aggregation kinetics for IgG1-based monoclonal antibody therapeutics. The AAPS journal, 2016, 18(3): 689-702. DOI: 10.1208/s12248-016-9887-0
Falke S, Betzel C. Dynamic light scattering (DLS) principles, perspectives, applications to biological samples. Radiation in bioanalysis: Spectroscopic techniques and theoretical methods, 2019: 173-193. DOI: 10.1007/978-3-030-28247-9_6
Jia Z, et al. Dynamic light scattering: a powerful tool for in situ nanoparticle sizing. Colloids and Interfaces, 2023, 7(1): 15. DOI: 10.3390/colloids7010015
Lyu T S, et al. The characterization of exosomes from fibrosarcoma cell and the useful usage of Dynamic Light Scattering (DLS) for their evaluation. PLoS One, 2021, 16(1): e0231994. DOI: 10.1371/journal.pone.0231994