Description
Bz-IEGR-pNA acetate is a colorimetric substrate for Factor Xa. Factor Xa preferentially binds to and cleaves the Ile-Glu-Gly-Arg (IEGR) peptide sequence to release p-nitroanilide (pNA), which can be quantified by colorimetric detection at 405 nm as a measure of Factor Xa activity.
Structure and conformation
The structure of Bz-IEGR-PNA Acetate is complex and contains several functional groups. One end consists of a benzoyl group (Bz), which is somewhat hydrophobic and can influence the molecule's interactions with other substances. The middle portion is a peptide composed of isoleucine (Ile), glutamic acid (Glu), glycine (Gly), and arginine (Arg), linked by peptide bonds.
Isoleucine has a long hydrophobic side chain that enhances the molecule's overall hydrophobicity.
Glutamic acid contains a carboxyl group, making it acidic.
Glycine has the simplest structure and is the smallest amino acid.
Arginine features a guanidinium group in its side chain, giving it strong basicity.
The peptide's amino acid sequence and structure determine its binding affinity to specific enzymes. The other end is attached to p-nitroaniline (PNA), whose nitro group is strongly electron-withdrawing, enabling this moiety to play a unique role in specific reactions. The entire molecule is conjugated with acetate to form Bz-IEGR-PNA Acetate; the acetate moiety may influence the compound's solubility and ionic properties in solution.
