First, the cyclic depsipeptides were synthesized from an amino acid (L-alanine) and hydroxy acid derivatives. The hydroxy acid derivatives used were chloroacetyl chloride, DL-2-bromopropionyl bromide, and DL-2-bromo-
n-butyryl bromide. The depsipeptides obtained were abbreviated to L-MMO, L-DMO, and L-MEMO, respectively, in the order of the hydroxy acid derivatives. The yields of these depsipeptides were in order of L-MMO<L-DMO<L-MEMO, depending on the difficulty in the cyclization of their precursors (linear amides). We have prepared homo- and copolymers of depsipeptides and ε-caprolactone (CL) using tin (II) octylate [Sn (Oct)
2] as a catalyst. The reactivity (polymerizability) of depsipeptide monomers decreased in the order: L-MMO>L-DMO>L-MEMO (the L-MEMO homopolymer was not obtained). This is probably due to the ease of coordination of these monomers to Sn (Oct)
2 catalyst. The thermal properties and NMR spectra of depsipeptide/CL copolymers revealed that these copolymers had random sequences. Finally, we have examined the biodegradability of the copolymers by enzymes (cholesterol esterase, Proteinase K) and activated sludge. The degradation of the copolymers by the esterase was not very high, and was little affected by the hydroxy acid unit of depsipeptide. But, the degradability of the copolymers by Proteinase K and activated sludge was considerably greater than that of CL homopolymer, and was in the order: coply (L-MMO/CL) <copoly (L-DMO/CL) <copoly (L-MEMO/CL). From the changes in some properties (molecular weight, composition, thermal properties) of copolymers before and after degradation by Proteinase K, it has become apparent that noncrystalline parts containing more depsipeptide in the copolymers were degraded preferentially. The measurement of the mechanical properties of the polymers indicated that these depsipeptide/CL copolymers have much the same tensile strength as that of high density polyethylene.
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