2 research outputs found
Influence of N<sub>ε</sub>‑Protecting Groups on the Protease-Catalyzed Oligomerization of l‑Lysine Methyl Ester
The direct oligomerization of l-lys-OMe by bromelain catalysis
gave oligoÂ(l-lys) with DP<sub>avg</sub> ∼ 3.6 and
dispersity ∼ 1.1. Since higher chain length oligoÂ(l-lys) with lower dispersity values and one reactive amine for selective
conjugation would be beneficial, we explored protease-catalyzed oligomerization
of N<sub>ε</sub>-protected l-lys monomers where N<sub>ε</sub>-groups included <i>tert</i>-butoxycarbonyl
(Boc) or benzyloxycarbonyl (Z) groups. By using N<sub>ε</sub>-protected l-lys monomers, oligopeptide side-chains are
hydrophobic-neutral which should dramatically alter enzyme kinetic
and binding constants relative to nonprotected l-lys. Schechter
and Berger’s conceptual model guided our choice of papain as
the protease catalyst. Papain-catalyzed oligomerization of N<sub>ε</sub>-Boc-l-Lys-OMe gave products with DP<sub>avg</sub> values
that were pH dependent and varied from 4.7 ± 0.2 to 7.5 ±
0.1. Similarly, oligoÂ(N<sub>ε</sub>-Z-l-Lys) synthesis
was pH dependent, and DP<sub>avg</sub> values varied from 4.3 ±
0.2 to 5 ± 0.2. OligoÂ(N<sub>ε</sub>-Boc/Z-l-Lys)
that precipitates from reaction media had a low dispersity (∼1.01).
The relatively smaller N<sub>ε</sub>-Boc group should increase
propagating chain solubility enabling oligopeptides to reach higher
DP<sub>avg</sub> values prior to their precipitation. Since papain-catalyzed
oligomerizations of N<sub>ε</sub>-Boc/Z-l-Lys proceeded
slowly at 0.54 mg/mL, higher enzyme concentrations were studied. By
increasing the enzyme concentration in oligomerizations from 0.54
to 1.62 mg/mL for 3 h reactions, the %-yield and DP<sub>avg</sub> of
oligoÂ(N<sub>ε</sub>-Z-l-lys) increased from 24 ±
0 to 88 ± 2 and 4.1 ± 0.7 to 5.7 ± 0.1, respectively.
Furthermore, at 1.89 mg/mL papain, the %-yield of oligoÂ(N<sub>ε</sub>-Z-l-lys) increased with time reaching 91% in 2 h. Acetonitrile
at 20%-by-volume was a useful cosolvent that increased the oligopeptide
yield and DP<sub>avg</sub> relative to reactions run in pure buffer
Poly(butylene 2,5-furan dicarboxylate), a Biobased Alternative to PBT: Synthesis, Physical Properties, and Crystal Structure
This paper describes the synthesis, crystal structure,
and physicomechanical
properties of a biobased polyester prepared from 2,5-furandicarboxylic
acid (FDCA) and 1,4-butanediol. Melt-polycondensation experiments
were conducted by a two-stage polymerization using titanium tetraisopropoxide
(TiÂ[OiPr]<sub>4</sub>) as a catalyst. Polymerization conditions (catalyst
concentration, reaction time and second stage reaction temperature)
were varied to optimize polyÂ(butylene-FDCA), PBF, and molecular weight.
A series of PBFs with different <i>M</i><sub>w</sub> were
characterized by DSC, TGA, DMTA, X-ray diffraction and tensile testing.
Influence of molecular weight and melting/crystallization enthalpy
on PBF material tensile properties was explored. Cold-drawing tensile
tests at room temperature for PBF with <i>M</i><sub>w</sub> 16K to 27K showed a brittle-to-ductile transition. When <i>M</i><sub>w</sub> reaches 38K, the Young modulus of PBF remains
above 900 MPa, and the elongation at break increases to above 1000%.
The mechanical properties, thermal properties and crystal structures
of PBF were similar to petroleum derived polyÂ(butylenes-terephthalate),
PBT. Fiber diagrams of uniaxially stretched PBF films were collected,
indexed, and the unit cell was determined as triclinic (<i>a</i> = 4.78(3) Å, <i>b</i> = 6.03(5) Å, <i>c</i> = 12.3(1) Å, α = 110.1(2)°, β = 121.1(3)°,
γ = 100.6(2)°). A crystal structure was derived from this
data and final atomic coordinates are reported. We concluded that
there is a close similarity of the PBF structure to PBT α- and
β-forms