TY - JOUR
T1 - Aliphatic Chain Modification of Collagen Type I
T2 - Development of Elastomeric, Compliant, and Suturable Scaffolds
AU - Yu, Christine
AU - Sharma, Shivang
AU - Fang, Chen Hao
AU - Jeong, Harrison
AU - Li, Jiuru
AU - Joice, Gregory
AU - Bivalacqua, Trinity J.
AU - Singh, Anirudha
N1 - Funding Information:
Funding sources gratefully acknowledged are the Johns Hopkins Greenberg Bladder Cancer award, Johns Hopkins Brady Urological Institute start-up funding, JHU-KKESH award, and NIH-NIBIB R21 trailblazer award. We also thank Dr. Brian Crawford of the Department of Materials Science and Engineering of Johns Hopkins University for allowing us to perform experiments on Instron tensile testing equipment. We also thank Katherine Tripp of Center for Molecular Biophysics of Johns Hopkins University for allowing us to perform circular dichroism experiments.
Publisher Copyright:
© 2020 American Chemical Society.
Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 2020/3/16
Y1 - 2020/3/16
N2 - Collagen type I is one of the most suitable natural biomaterials for constructing tissue-engineering scaffolds. Despite their biocompositional similarities to physiological tissues, these scaffolds lack host specific and matching mechanical properties. While it is possible to enhance their stiffness by cross-linking, it often compromises their abilities to expand or strain under minimal stress, that is, compliance (inverse of stiffness). Here, we report a simple, inexpensive, cross-linking-and elastin-free collagen-based material composition for developing elastomeric scaffolds that are highly compliant, soft yet strong, and suturable, therefore, clinically attractive. Our strategy utilizes roomerature modification of collagen type I scaffolds with linear aliphatic chains of various lengths (C7-C18). In particular, dodecenylsuccinic anhydride (size: C12, DDSA) modified scaffolds elongated up to 400% of its initial length compared to only ∼20% for collagen-control within the applied tensile stress of 0.2 MPa without breaking. Furthermore, the suture retention strength value increased to 60 g-force from 30 g-force for collagen control. We confirmed that the C12-modified material remained structurally stable at the physiological temperature (37 °C) with a tan δvalue of ∼0.3, similar to collagen control; however, tan δincreased sharply for C12-modified collagen above 42 °C, compared to 59 °C for collagen control. To understand the mechanism of hyperextensibility, we studied the morphology of the resultant material by transmission electron microscopy (TEM), which showed an altered microstructure of C12-modified collagen scaffolds. While the partially C12-modified sample had a mixture of typical collagen type I triple helix and diffused gelatinized random coil-like configuration, the fully modified samples showed thick wrinkled and entangled ribbon-like microstructures, which was different than that of thermally denatured gelatin. We further confirmed that the resultant material allowed cell growth in vitro and in vivo in a subcutaneous mouse model.
AB - Collagen type I is one of the most suitable natural biomaterials for constructing tissue-engineering scaffolds. Despite their biocompositional similarities to physiological tissues, these scaffolds lack host specific and matching mechanical properties. While it is possible to enhance their stiffness by cross-linking, it often compromises their abilities to expand or strain under minimal stress, that is, compliance (inverse of stiffness). Here, we report a simple, inexpensive, cross-linking-and elastin-free collagen-based material composition for developing elastomeric scaffolds that are highly compliant, soft yet strong, and suturable, therefore, clinically attractive. Our strategy utilizes roomerature modification of collagen type I scaffolds with linear aliphatic chains of various lengths (C7-C18). In particular, dodecenylsuccinic anhydride (size: C12, DDSA) modified scaffolds elongated up to 400% of its initial length compared to only ∼20% for collagen-control within the applied tensile stress of 0.2 MPa without breaking. Furthermore, the suture retention strength value increased to 60 g-force from 30 g-force for collagen control. We confirmed that the C12-modified material remained structurally stable at the physiological temperature (37 °C) with a tan δvalue of ∼0.3, similar to collagen control; however, tan δincreased sharply for C12-modified collagen above 42 °C, compared to 59 °C for collagen control. To understand the mechanism of hyperextensibility, we studied the morphology of the resultant material by transmission electron microscopy (TEM), which showed an altered microstructure of C12-modified collagen scaffolds. While the partially C12-modified sample had a mixture of typical collagen type I triple helix and diffused gelatinized random coil-like configuration, the fully modified samples showed thick wrinkled and entangled ribbon-like microstructures, which was different than that of thermally denatured gelatin. We further confirmed that the resultant material allowed cell growth in vitro and in vivo in a subcutaneous mouse model.
KW - bioelastomer
KW - collagen
KW - compliance
KW - hyperextensible
KW - rubber
KW - scaffolds
KW - suture strength
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U2 - 10.1021/acsabm.9b00781
DO - 10.1021/acsabm.9b00781
M3 - Article
AN - SCOPUS:85080134440
VL - 3
SP - 1331
EP - 1343
JO - ACS Applied Bio Materials
JF - ACS Applied Bio Materials
SN - 2576-6422
IS - 3
ER -