The resultant NMR spectra confirmed the degradation products to be of the same

structure. Degradation was expected based on previous research that indicated the

alaninol polymer was readily degradable.6 The degradation observed in the phosphate

buffer solution suggests the alaninol polymer is degradable at pH 7.2. The polymer itself

must be somewhat pH sensitive. The complete degradation of the alaninol polymer (14)

by trypsin proved to be the only example of total degradation in these experiments. This

is likely related to the high concentration of the enzyme and the high degradability of the

alaninol polymer (14).

 The lack of discernable degradation in the isoleucinol and phenylalaninol polymers

is intriguing. These polymers present unique problems for the enzymes to overcome. If,

in fact, the solvent-crystallized structure for the phenylalaninol polymer (18) were greatly

influenced by the aromatic side chain this influence would need to be overcome in order

for degradation to occur. The isoleucinol (17) side chain is hydrophobic enough to

prevent an aqueous enzyme from gaining the access necessary for recognition and bond

breaking. The active site on the enzymes may prove unable to recognize the hydrophobic

side chain in the midst of such a hydrophobic backbone. These two polymers may also

represent cases of polymers being too insoluble to allow degradation.

 In conclusion, the 8-spacer monomers (1-6) can be successfully polymerized using

the 2nd generation Grubbs' catalyst to make high molecular weight polymer. These

biologically based polymers have shown good material properties consistent with other

polycondensation polymers. The unsaturated polymers were successfully hydrogenated

using a homogeneous catalyst (Wilkinson's catalyst). The resultant polymers (13-18)

represent the first ADMET polymers subjected to enzymatic degradation. These