Journal
BIOMACROMOLECULES
Volume 13, Issue 4, Pages 1100-1105Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm201847n
Keywords
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Funding
- Nanoscale Science and Engineering Center at UW-Madison [DMR-0832760]
- NIH [R21EB013259]
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [832760] Funding Source: National Science Foundation
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Nylon-3 polymers have a polyamide backbone reminiscent of that found in proteins (beta- vs alpha-amino acid residues, respectively), which makes these materials interesting for biological applications. Because of the versatility of the ring-opening polymerization process and the variety of beta-lactam starting materials available, the structure of nylon-3 copolymers is highly amenable to alteration. A previous study showed that relatively subtle changes in the structure or ratio of hydrophobic and cationic subunits that comprise these polymers can result in significant changes in the ability of nylon-3-bearing surfaces to support cell adhesion and spreading. In the present study, we have exploited the highly tailorable nature of these polymers to synthesize new versions possessing a wide range of chain lengths, with the intent of optimizing these materials for use as cell-supportive substrates. We find that longer nylon-3 chains lead to better fibroblast attachment on modified surfaces and that at the optimal chain lengths less hydrophobic subunits are superior. The best polymers we identified are comparable to an RGD-containing peptide in supporting fibroblast attachment. The results described here will help to focus future efforts aimed at relining nylon-3 copolymer substrates for specific tissue engineering applications.
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