Zwitterionic Detergents Line

Zwitterionic detergents are a class of surfactants that contain both positively and negatively charged groups, exhibiting characteristics of both anionic and cationic surfactants. They offer the advantages of mildness, stability, and high compatibility. In membrane protein research, these detergents can efficiently solubilize cell membranes, maintain the native conformation of membrane proteins, and ensure that protein activity is preserved throughout extraction, purification, and functional studies.

As a specialized supplier of detergents, Alfa Chemistry provides high-purity, high-performance zwitterionic detergents specifically designed for membrane protein extraction and functional research, along with comprehensive technical support and customized solutions for scientific customers.

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Introduction to Zwitterionic Detergents

Zwitterionic detergents are a class of surfactants that contain both cationic and anionic groups within the same molecule. This unique molecular structure allows them to exhibit self-regulated charge states in aqueous solutions, resulting in mild yet highly efficient solubilization and cleaning capabilities. Common types include:

Betaine-based detergents: Mild and highly compatible, suitable for sensitive systems.
Sulfobetaines: Provide fine foam and excellent emulsification properties, ideal for membrane protein extraction.
Amine oxides: High cleaning power, effective for solubilizing lipid membranes and multi-pass membrane proteins.

Compared with anionic, cationic, or nonionic detergents, zwitterionic detergents offer superior mildness, enhanced preservation of membrane protein activity, and better compatibility with complex biological systems.

Product Specifications and Performance

Alfa Chemistry’s amphoteric detergents feature strict technical parameters and reliable performance, including:

Appearance and Physical Properties

Liquid or paste, transparent or light yellow.

Active Content

Customizable according to customer requirements.

pH Range

5–9, with strong buffering capacity suitable for experimental systems.

Emulsification and Cleaning Performance

Capable of dissolving lipid membranes and protein precipitates.

Biocompatibility

Low toxicity, does not disrupt proteins or membrane protein functions.

Stability

Maintains stable performance under variations in temperature, salt concentration, and pH.

Applications of Zwitterionic Detergents

Membrane Protein Extraction

Efficiently solubilize cell membranes and tissue membranes to obtain intact membrane proteins.
Gentle on multi-transmembrane proteins and lipid-binding proteins.

Membrane Protein Functional Studies

Preserve the native conformation of proteins, ensuring reliable experimental results.
Suitable for structural biology research, drug target analysis, and mechanism studies.

Protein Purification

Compatible with affinity chromatography, gel filtration, and ion exchange techniques.
Provide a stable environment to prevent membrane protein aggregation or inactivation.

Pharmaceutical and Biomedical Research

Applied in membrane protein-related processes for vaccine preparation and drug formulations.
Maintain protein activity and emulsification efficiency while ensuring safety.

Alfa Chemistry Product Advantages

Our zwitterionic detergents are designed to provide reliable performance, flexibility, and expert support, ensuring success in diverse membrane protein research applications.

High-purity raw materials

Ensure stability and reproducibility in membrane protein experiments.

Multiple specifications available

Customized concentrations and formats tailored to different membrane protein types.

Technical support

Assistance with experimental protocol optimization, formulation guidance, and membrane protein application consulting.

Strict quality control

Guarantee consistent performance across batches to meet research needs.

Customers Often Look For

Here are some of the most frequently selected zwitterionic detergents that researchers rely on for membrane protein studies and related applications.

n-Dodecyl-N,N-dimethylglycine

CHAPS

Sulfobetaine-10

Lauryldimethylamine oxide (LDAO)

n-Dodecyl-N,N-dimethylglycine

CAS 683-10-3

A zwitterionic detergent with strong solubilization capacity and protein-stabilizing properties.

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CHAPS

CAS 75621-03-3

A betaine-type detergent, highly effective in solubilizing lipid membranes while preserving protein activity.

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Sulfobetaine-10

CAS 15163-36-7

A sulfo-betaine detergent with strong compatibility, suitable for use in complex buffer systems.

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Lauryldimethylamine oxide (LDAO)

CAS 1643-20-5

An amine oxide detergent with strong cleaning capability, commonly applied in membrane protein structural studies.

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Comprehensive Zwitterionic Detergent Services

Alfa Chemistry provides comprehensive zwitterionic detergent-related services to support researchers in optimizing membrane protein experimental workflows:

Detergent Characterizations

Characterization of physicochemical properties, emulsification, and foaming performance.

Structural Characterization

Physicochemical Properties Characterization

Detergents Selection

Recommending the most suitable detergents based on membrane protein types and experimental systems.

Detergents Design

Designing detergents with special structures or blends tailored to customer needs, aiming to optimize performance.

Custom Services

Providing customized concentrations, specifications, and large-scale production to meet diverse research and industrial requirements.

What Success Stories Can We Share?

Discover how our products are applied in real-world scenarios through our case studies.

Case 1: A Biochemistry Research Institute in Germany

Background

This institute has long been engaged in membrane protein research and required a mild yet efficient detergent to extract and stabilize membrane proteins. In the past, they tested several nonionic detergents, but encountered problems with protein stability and experimental reproducibility.

Procurement and Application

After comparing products from multiple suppliers, the research team purchased n-Dodecyl-N,N-dimethylglycine from our company. They found that this zwitterionic detergent not only maintained protein activity but also effectively improved solubility and significantly reduced sample degradation.

Experimental Data

Protein extraction yield: increased from 62% ± 3% to 89% ± 2%
Protein activity retention (after 48 hours): improved from 70% to 93%
Sample degradation rate: reduced from 18% to<5%
Cryo-EM resolution: improved from 4.2 Å to 3.3 Å

Result

The institute reported that after using this product, they achieved higher resolution in cryo-EM structural analysis, improved stability of protein complexes, and ultimately succeeded in publishing a high-impact academic paper.

Case 2: An Enzyme Research Laboratory at a U.S. University

Background

A well-known university in Boston, USA, has a biochemistry laboratory focused on the functional study of hydrolases and transport proteins. During high-throughput screening and enzyme kinetics experiments, the researchers found that traditional nonionic or anionic detergents had limitations in maintaining protein activity and solubility, with some enzymes showing significant loss of activity during processing.

Procurement and Application

The laboratory purchased CHAPS (a zwitterionic detergent) from our company, which was used to extract and stabilize hydrolases. They also incorporated it into the buffer system for 96-well high-throughput enzyme activity screening, aiming to reduce nonspecific adsorption and enzyme inactivation. The research team optimized the detergent concentration (0.5%–1% w/v) to achieve the best performance.

Experimental Data

Enzyme extraction yield (vs. control without detergent): increased from 61% ± 3% to 88% ± 2%
Enzyme activity retention (after 24 hours at room temperature): improved from 72% to 95%
High-throughput screening reproducibility (RSD): reduced from 12% to 4%
Protein solubility: increased from 0.7 mg/mL to 1.5 mg/mL
Nonspecific adsorption: reduced by approximately 60%

Result

The research team stated that the application of CHAPS significantly improved enzyme activity retention and experimental reproducibility, making the high-throughput screening data much more reliable. This provided a solid foundation for enzyme function studies and inhibitor screening. They have since adopted this detergent as a standard reagent for long-term use and mentioned the method in their recent publications.

Case 3: A Pharmaceutical Company in the United Kingdom

Background

This company is developing a liposome-based drug delivery system, requiring a detergent that can act as a stabilizer during formulation while also ensuring good biocompatibility during drug release.

Procurement and Application

The company purchased our Lauryl sulfobetaine. In experiments, the R&D team found that this detergent exhibited excellent emulsification and stabilization effects during liposome preparation. The resulting liposomes had uniform particle sizes and high encapsulation efficiency.

Experimental Data

Average particle size (measured by DLS): 128 ± 5 nm (coefficient of variation<5%)
Encapsulation efficiency (using peptide drug as a model): increased from 68% with traditional methods to 87%
Particle size stability: stored at 4 °C for 30 days, size variation<10 nm, no obvious aggregation
In vitro release test: in PBS (pH 7.4, 37 °C), 24-hour release rate of 72%, with no cytotoxic response (cell viability >95%)

Result

The new formulation successfully passed early-stage in vitro studies. The client reported that the use of this detergent saved significant development time and greatly improved the success rate of the project.

Frequently Asked Questions (FAQ)

Q1. How do zwitterionic detergents balance solubilization and protein stability in membrane protein extraction?

A: Zwitterionic detergents such as CHAPS or n-Dodecyl-N,N-dimethylglycine possess hydrophilic head groups carrying both positive and negative charges, while their hydrophobic tails create a microenvironment to solubilize membrane proteins. At the same time, they minimize strong electrostatic interactions that could cause protein denaturation. The optimal concentration and temperature should be adjusted according to the hydrophobicity of the target protein and the sensitivity of the protein complex. In addition, protein aggregation should be monitored using dynamic light scattering (DLS) or size-exclusion chromatography (SEC) to ensure a proper balance between solubilization efficiency and structural stability.

Q2. What impact do zwitterionic detergents have on downstream structural analysis methods (cryo-EM, NMR)?

A: When forming protein–detergent complexes, zwitterionic detergents typically produce uniform micelles, which reduce nonspecific aggregation, thereby improving sample homogeneity and signal-to-noise ratio. For NMR, high detergent concentrations may broaden spectral lines, so the detergent concentration should be optimized below the critical micelle concentration (CMC) to maintain resolvable signals. For cryo-EM, micelle size can be controlled through gradient concentration adjustment or buffer optimization to achieve better particle distribution and higher resolution.

Q3. How can protein inactivation or aggregation be prevented when using zwitterionic detergents?

A: Preventing protein inactivation should be considered from three aspects:

Concentration control: Maintain detergent concentration slightly above the protein solubilization threshold but below the level where oversized micelles form and cause nonspecific interactions.
Temperature control: Conduct experiments at low temperatures (4–10 °C) to minimize protein degradation.
Additive combination: Add glycerol, NaCl, or appropriate buffer systems to stabilize protein folding and shield surface charges, thereby reducing aggregation and nonspecific adsorption.

Q4. How do zwitterionic detergents affect particle size and stability in liposome or nanoparticle preparation?

A: Zwitterionic detergents reduce interfacial tension through their surface activity while forming a stable amphiphilic molecular layer, which regulates particle size and distribution. In practice, dynamic light scattering (DLS) can be used to determine particle size distribution, and the detergent-to-lipid ratio (w/w) can be adjusted to achieve uniform particle size. Moreover, stability is strongly dependent on the ionic strength, pH, and temperature of the buffer system, which should be systematically optimized prior to preparation.

Q5. What is the compatibility of zwitterionic detergents with protein purification chromatography?

A: Zwitterionic detergents generally do not strongly interfere with anion or cation exchange chromatography, but they may influence selectivity in hydrophobic interaction chromatography (HIC) or affinity chromatography. Recommended practices include:

Pre-washing column resins to remove impurities.
Optimizing detergent concentration to minimize nonspecific adsorption while maintaining solubility of the target protein.
Applying stepwise dilution or gradient elution strategies when necessary, to avoid interference from protein–detergent complexes and ensure purification efficiency.

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