Jump to content

Trypsin chiral specificity

Recommended Posts

From: All-D amino acid-containing channel-forming antibiotic peptides

"The resistance of L- and D-cecropin A to enzymatic cleavage by the enzymes trypsin and InA (15) is illustrated in Fig.

3 Upper and Lower, respectively. The all-L peptide was

hydrolyzed and inactivated rapidly by trypsin (50% in 20 min

at a peptide-to-enzyme weight ratio of 2500: 1) or by InA (50%o

in 20 min at a ratio of 200:1). In sharp contrast, the all-D

peptide was completely stable to both enzymes, up to a

concentration of trypsin 2000 times higher than needed for

50%o inactivation of the L peptide. In addition, experiments in

rabbit serum showed that L-cecropin A was 50% degraded in

2 hr, whereas the D enantiomer was much more stable

(half-time for loss of activity, 30 hr)."

So, it looks like yes.

Share this post

Link to post
Share on other sites

Create an account or sign in to comment

You need to be a member in order to leave a comment

Create an account

Sign up for a new account in our community. It's easy!

Register a new account

Sign in

Already have an account? Sign in here.

Sign In Now

  • Create New...

Important Information

We have placed cookies on your device to help make this website better. You can adjust your cookie settings, otherwise we'll assume you're okay to continue.