TY - JOUR
T1 - Visualizing the Inner Architecture of Poly(ε-caprolactone)-Based Biomaterials and Its Impact on Performance Optimization
AU - Bauer, Adam J.P.
AU - Wu, Yitian
AU - Liu, Jianzhao
AU - Li, Bingbing
N1 - Publisher Copyright:
© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
PY - 2015/11/1
Y1 - 2015/11/1
N2 - The performance of poly(ε-caprolactone) (PCL)-based biomaterials is defined by spatial distributions of PCL's amorphous and crystalline domains. Unfortunately, directly visualizing their inner architectures has been challenging. This study demonstrates, the superior degradation selectivity of Candida antarctica lipase B (CALB) enzyme; when used at low concentrations, it preferentially breaks down the amorphous chains prior to the crystalline chains. Top-down dissection using this enzyme is performed on several PCL-based systems. Self-assembled nanolamellae (e.g., thin films) or hierarchically nanostructured crystalline skeletons (e.g., fibers) are clearly captured. Thus, the spatial distribution of the amorphous compartments can be precisely mapped out, which otherwise cannot be achieved. The superior degradation selectivity of Candida antarctica lipase B (CALB) enzyme is demonstrated. When used at low concentrations, it preferentially breaks down the amorphous chains of poly(ε-caprolactone) (PCL) prior to its crystalline chains. Top-down dissection using this enzyme is performed on several PCL-based model systems. The spatial distribution of the amorphous compartments are precisely mapped out, which otherwise cannot be achieved.
AB - The performance of poly(ε-caprolactone) (PCL)-based biomaterials is defined by spatial distributions of PCL's amorphous and crystalline domains. Unfortunately, directly visualizing their inner architectures has been challenging. This study demonstrates, the superior degradation selectivity of Candida antarctica lipase B (CALB) enzyme; when used at low concentrations, it preferentially breaks down the amorphous chains prior to the crystalline chains. Top-down dissection using this enzyme is performed on several PCL-based systems. Self-assembled nanolamellae (e.g., thin films) or hierarchically nanostructured crystalline skeletons (e.g., fibers) are clearly captured. Thus, the spatial distribution of the amorphous compartments can be precisely mapped out, which otherwise cannot be achieved. The superior degradation selectivity of Candida antarctica lipase B (CALB) enzyme is demonstrated. When used at low concentrations, it preferentially breaks down the amorphous chains of poly(ε-caprolactone) (PCL) prior to its crystalline chains. Top-down dissection using this enzyme is performed on several PCL-based model systems. The spatial distribution of the amorphous compartments are precisely mapped out, which otherwise cannot be achieved.
KW - electrospinning
KW - morphology
KW - poly(ε-caprolactone)
KW - secondary nanostructures
UR - http://www.scopus.com/inward/record.url?scp=84946472877&partnerID=8YFLogxK
U2 - 10.1002/mabi.201500175
DO - 10.1002/mabi.201500175
M3 - Article
C2 - 26154435
AN - SCOPUS:84946472877
VL - 15
SP - 1554
EP - 1562
JO - Macromolecular Bioscience
JF - Macromolecular Bioscience
SN - 1616-5187
IS - 11
ER -