Does anyone know if trypsin can cleave D-form peptides, i.e., c-terminal to a D-arginine or D-lysine?

I don't know exactly, but given how specific trypsin is, I would say it probably cleaves L-amino acids exclusively.

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.