Journal
BIOMACROMOLECULES
Volume 12, Issue 7, Pages 2573-2582Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm200368p
Keywords
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Funding
- NSF [CHE-0965060, CHE-9977144, DMR-0821313]
- Cleveland Clinic Foundation/Clinical Tissue Engineering Center [TECH-09-006A]
- NSF at the University of Akronh [DMR-0648318]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0965060] Funding Source: National Science Foundation
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [0821313] Funding Source: National Science Foundation
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A new type of polymer highly resistant to nonspecific protein adsorption is reported. Poly(N-methyl-beta-alanine) (PMeA) and poly(N-ethyl-beta-alanine) (PEtA) synthesized via cobalt-catalyzed carbonylative polymerization of N-methylaziridine and N-ethylaziridine were end-functionalized with thiol groups and grafted onto Au surfaces. Protein adsorption was studied by the surface plasmon resonance (SPR) method. The amounts of representative single proteins adsorbed onto the PMeA- and PEtA-grafted surfaces were below the detection limit of SPR at the pg/mm(2) level. After exposure to full blood plasma and serum for 10 min, protein adsorption was at the level of similar to 100 pg/mm(2), similar to the level of protein adsorption on poly(ethylene glycol) surfaces subjected to identical conditions. These poly(beta-peptoid)s therefore provide excellent protein resistance comparable to the best antifouling materials known to date. The strong proton-accepting ability when forming hydrogen bonds is suggested to be an important attribute for these poly(beta-peptoid)s as well as other poly(tertiary amide)s as antifouling materials.
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