Mal-PEG-alcohol contains a maleimide functional group (-Mal) attached to one end of a PEG chain, and an alcohol functional group (-OH) attached to the other end.
The maleimide group is known for its ability to react with thiol groups (-SH) on proteins and peptides, forming stable thioether bonds. This unique chemical property of Mal-PEG-alcohol makes it a useful tool in the field of pharmaceutical research and development.
Mal-PEG-alcohol has been extensively utilized in the development of site-specific protein conjugation and labeling techniques. The maleimide group on Mal-PEG-alcohol reacts selectively with thiol groups on proteins and peptides, allowing for the covalent attachment of various molecules, such as fluorescent dyes or drugs, to specific sites on the protein. This enables the creation of conjugates with improved properties such as increased stability, solubility, and targeted delivery.