The Effect of Surface Modification of Aligned Poly-L-Lactic Acid Electrospun Fibers on Fiber Degradation and Neurite Extension.
The surface of aligned, electrospun poly-L-lactic acid (PLLA) fibers was chemically modified to determine if surface chemistry and hydrophilicity could improve neurite extension from chick dorsal root ganglia. Specifically, diethylenetriamine (DTA, for amine functionalization), 2-(2-aminoethoxy)ethanol (AEO, for alcohol functionalization), or GRGDS (cell adhesion peptide) were covalently attached to the surface of electrospun fibers. Water contact angle measurements revealed that surface modification of electrospun fibers significantly improved fiber hydrophilicity compared to unmodified fibers (p < 0.05). Scanning electron microscopy (SEM) of fibers revealed that surface modification changed fiber topography modestly, with DTA modified fibers displaying the roughest surface structure. Degradation of chemically modified fibers revealed no change in fiber diameter in any group over a period of seven days. Unexpectedly, neurites from chick DRG were longest on fibers without surface modification (1651 ± 488 μm) and fibers containing GRGDS (1560 ± 107 μm). Fibers modified with oxygen plasma (1240 ± 143 μm) or DTA (1118 ± 82 μm) produced shorter neurites than the GRGDS or unmodified fibers, but were not statistically shorter than unmodified and GRGDS modified fibers. Fibers modified with AEO (844 ± 151 μm) were significantly shorter than unmodified and GRGDS modified fibers (p<0.05). Based on these results, we conclude that fiber hydrophilic enhancement alone on electrospun PLLA fibers does not enhance neurite outgrowth. Further work must be conducted to better understand why neurite extension was not improved on more hydrophilic fibers, but the results presented here do not recommend hydrophilic surface modification for the purpose of improving neurite extension unless a bioactive ligand is used.
Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180-3590, United States of America; Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY, 12180-3590, United States of America.
Nicholas J
NJ
Schaub
Institut Charles Gerhardt de Montpellier, UMR 5253, CNRS-UM-ENSCM, Université de Montpellier, CC 1701, Place E. Bataillon, F-34095 Montpellier cedex 05, France.
Clémentine
C
Le Beux
Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180-3590, United States of America; Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, 110 8th Street, Troy, NY, 12180-3590, United States of America.
Jianjun
J
Miao
Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180-3590, United States of America; Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY, 12180-3590, United States of America; Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, 110 8th Street, Troy, NY, 12180-3590, United States of America; Department of Biology, Rensselaer Polytechnic Institute, 110 8th Street, Troy, NY, 12180-3590, United States of America; Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY, 12180-3590, United States of America.
Robert J
RJ
Linhardt
Institut Charles Gerhardt de Montpellier, UMR 5253, CNRS-UM-ENSCM, Université de Montpellier, CC 1701, Place E. Bataillon, F-34095 Montpellier cedex 05, France.
Johan G
JG
Alauzun
Institut Charles Gerhardt de Montpellier, UMR 5253, CNRS-UM-ENSCM, Université de Montpellier, CC 1701, Place E. Bataillon, F-34095 Montpellier cedex 05, France.
Danielle
D
Laurencin
Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180-3590, United States of America; Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY, 12180-3590, United States of America.
Ryan J
RJ
Gilbert
D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry / Q000494:pharmacology*; D002448:Cell Adhesion / Q000187:drug effects; D002645:Chickens; D000431:Ethanol / Q000031:analogs & derivatives / Q000737:chemistry; D005021:Ethylamines / Q000737:chemistry; D005727:Ganglia, Spinal / Q000166:cytology / Q000187:drug effects* / Q000502:physiology; D057927:Hydrophobic and Hydrophilic Interactions; D019344:Lactic Acid / Q000737:chemistry / Q000494:pharmacology*; D009416:Nerve Regeneration / Q000502:physiology; D016501:Neurites / Q000187:drug effects* / Q000502:physiology; D009842:Oligopeptides / Q000737:chemistry; D058626:Plasma Gases / Q000737:chemistry; D011073:Polyamines / Q000737:chemistry; D011091:Polyesters; D011108:Polymers / Q000737:chemistry / Q000494:pharmacology*; D013499:Surface Properties; D046509:Tissue Culture Techniques; D023822:Tissue Engineering; D054457:Tissue Scaffolds
D001672:Biocompatible Materials; D005021:Ethylamines; D009842:Oligopeptides; D058626:Plasma Gases; D011073:Polyamines; D011091:Polyesters; D011108:Polymers; C005391:diethylenetriamine; D019344:Lactic Acid; D000431:Ethanol; C033616:poly(lactide); C110684:2-(2-aminoethoxy)ethanol; C049554:glycyl-arginyl-glycyl-aspartyl-serine