TheAngryPenguin Posted July 30, 2013 Share Posted July 30, 2013 Does anyone know if trypsin can cleave D-form peptides, i.e., c-terminal to a D-arginine or D-lysine? Link to comment Share on other sites More sharing options...
hypervalent_iodine Posted July 30, 2013 Share Posted July 30, 2013 I don't know exactly, but given how specific trypsin is, I would say it probably cleaves L-amino acids exclusively. Link to comment Share on other sites More sharing options...
Maximilian Posted August 4, 2013 Share Posted August 4, 2013 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. Link to comment Share on other sites More sharing options...
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