TY - JOUR
T1 - Structural evolution of photocrosslinked silk fibroin and silk fibroin-based hybrid hydrogels
T2 - A small angle and ultra-small angle scattering investigation
AU - Whittaker, Jasmin L.
AU - Balu, Rajkamal
AU - Knott, Robert
AU - de Campo, Liliana
AU - Mata, Jitendra P.
AU - Rehm, Christine
AU - Hill, Anita J.
AU - Dutta, Naba K.
AU - Roy Choudhury, Namita
N1 - Publisher Copyright:
© 2018
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 2018/7/15
Y1 - 2018/7/15
N2 - Regenerated Bombyx mori silk fibroin (RSF) is a widely recognized protein for biomedical applications; however, its hierarchical gel structure is poorly understood. In this paper, the hierarchical structure of photocrosslinked RSF and RSF-based hybrid hydrogel systems: (i) RSF/Rec1-resilin and (ii) RSF/poly(N-vinylcaprolactam (PVCL) is reported for the first time using small-angle scattering (SAS) techniques. The structure of RSF in dilute to concentrated solution to fabricated hydrogels were characterized using small angle X-ray scattering (SAXS), small angle neutron scattering (SANS) and ultra-small angle neutron scattering (USANS) techniques. The RSF hydrogel exhibited three distinctive structural characteristics: (i) a Porod region in the length scale of 2 to 3 nm due to hydrophobic domains (containing β-sheets) which exhibits sharp interfaces with the amorphous matrix of the hydrogel and the solvent, (ii) a Guinier region in the length scale of 4 to 20 nm due to hydrophilic domains (containing turns and random coil), and (iii) a Porod-like region in the length scale of few micrometers due to water pores/channels exhibiting fractal-like characteristics. Addition of Rec1-resilin or PVCL to RSF and subsequent crosslinking systematically increased the nanoscale size of hydrophobic and hydrophilic domains, whereas decreased the homogeneity of pore size distribution in the microscale. The presented results have implications on the fundamental understanding of the structure–property relationship of RSF-based hydrogels.
AB - Regenerated Bombyx mori silk fibroin (RSF) is a widely recognized protein for biomedical applications; however, its hierarchical gel structure is poorly understood. In this paper, the hierarchical structure of photocrosslinked RSF and RSF-based hybrid hydrogel systems: (i) RSF/Rec1-resilin and (ii) RSF/poly(N-vinylcaprolactam (PVCL) is reported for the first time using small-angle scattering (SAS) techniques. The structure of RSF in dilute to concentrated solution to fabricated hydrogels were characterized using small angle X-ray scattering (SAXS), small angle neutron scattering (SANS) and ultra-small angle neutron scattering (USANS) techniques. The RSF hydrogel exhibited three distinctive structural characteristics: (i) a Porod region in the length scale of 2 to 3 nm due to hydrophobic domains (containing β-sheets) which exhibits sharp interfaces with the amorphous matrix of the hydrogel and the solvent, (ii) a Guinier region in the length scale of 4 to 20 nm due to hydrophilic domains (containing turns and random coil), and (iii) a Porod-like region in the length scale of few micrometers due to water pores/channels exhibiting fractal-like characteristics. Addition of Rec1-resilin or PVCL to RSF and subsequent crosslinking systematically increased the nanoscale size of hydrophobic and hydrophilic domains, whereas decreased the homogeneity of pore size distribution in the microscale. The presented results have implications on the fundamental understanding of the structure–property relationship of RSF-based hydrogels.
KW - Hierarchical structure
KW - Hybrid hydrogel
KW - Poly(N-vinylcaprolactam)
KW - Rec1-resilin
KW - Silk fibroin
KW - Small-angle scattering
UR - http://www.scopus.com/inward/record.url?scp=85045041595&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2018.03.044
DO - 10.1016/j.ijbiomac.2018.03.044
M3 - 文章
C2 - 29545061
AN - SCOPUS:85045041595
VL - 114
SP - 998
EP - 1007
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
SN - 0141-8130
ER -