Cymal detergents, short for "Cholate-based Detergents with Aromatic Side-chain Molecules," represent a class of detergents with unique properties tailored for membrane protein research. These detergents have a cholate-based structure combined with aromatic side-chain molecules, providing a distinctive blend of hydrophobic and hydrophilic characteristics.

Types of Cymal Detergents:

• Cymal-5 (5-Cyclohexyl-1-pentyl-β-D-maltoside): Cymal-5 is one of the well-known members of the cymal detergent family. It is characterized by a cyclohexyl group in the hydrophobic tail and a β-D-maltoside head group. Cymal-5 is valued for its ability to effectively solubilize membrane proteins while maintaining their native structure. The cyclohexyl moiety enhances the hydrophobic interactions, contributing to the stability of membrane protein complexes.

• Cymal-6 (6-Cyclohexyl-1-hexyl-β-D-maltoside): Cymal-6 is another variant within the cymal detergent family, featuring a longer alkyl chain compared to Cymal-5. The extended hydrophobic tail of Cymal-6 enhances its solubilizing capabilities and makes it suitable for a broader range of membrane protein targets. The incorporation of a cyclohexyl group maintains the balance between hydrophobicity and stability, making it a versatile choice for membrane protein studies.

Significance in Membrane Protein Research:

Cymal detergents have gained prominence in membrane protein research due to their unique combination of properties. The cholate-based structure contributes to the amphipathic nature of these detergents, allowing them to effectively interact with both hydrophobic membrane regions and hydrophilic protein surfaces.

The aromatic side-chain molecules in cymal detergents, such as the cyclohexyl groups in Cymal-5 and Cymal-6, provide increased stability to the detergent micelles, making them well-suited for solubilizing and stabilizing membrane proteins. This stability is particularly advantageous in applications such as structural studies and spectroscopy, where maintaining the integrity of membrane protein complexes is crucial.