Document Detail

An experimental-theoretical analysis of protein adsorption on peptidomimetic polymer brushes.
MedLine Citation:
PMID:  22107438     Owner:  NLM     Status:  MEDLINE    
Surface-grafted water-soluble polymer brushes are being intensely investigated for preventing protein adsorption to improve biomedical device function, prevent marine fouling, and enable applications in biosensing and tissue engineering. In this contribution, we present an experimental-theoretical analysis of a peptidomimetic polymer brush system with regard to the critical brush density required for preventing protein adsorption at varying chain lengths. A mussel adhesive-inspired DOPA-Lys (DOPA = 3,4-dihydroxy-phenylalanine; Lys = lysine) pentapeptide surface grafting motif enabled aqueous deposition of our peptidomimetic polypeptoid brushes over a wide range of chain densities. Critical densities of 0.88 nm(-2) for a relatively short polypeptoid 10-mer to 0.42 nm(-2) for a 50-mer were identified from measurements of protein adsorption. The experiments were also compared with the protein adsorption isotherms predicted by a molecular theory. Excellent agreements in terms of both the polymer brush structure and the critical chain density were obtained. Furthermore, atomic force microscopy (AFM) imaging is shown to be useful in verifying the critical brush density for preventing protein adsorption. The present coanalysis of experimental and theoretical results demonstrates the significance of characterizing the critical brush density in evaluating the performance of an antifouling polymer brush system. The high fidelity of the agreement between the experiments and molecular theory also indicate that the theoretical approach presented can aid in the practical design of antifouling polymer brush systems.
K H Aaron Lau; Chunlai Ren; Sung Hyun Park; Igal Szleifer; Phillip B Messersmith
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-12-08
Journal Detail:
Title:  Langmuir : the ACS journal of surfaces and colloids     Volume:  28     ISSN:  1520-5827     ISO Abbreviation:  Langmuir     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2012-01-31     Completed Date:  2012-05-23     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  9882736     Medline TA:  Langmuir     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2288-98     Citation Subset:  IM    
Copyright Information:
© 2011 American Chemical Society
Department of Biomedical Engineering, Northwestern University, Evanston, Illinois 60208, USA.
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MeSH Terms
Fibrinogen / chemistry*
Models, Molecular*
Peptidomimetics / chemistry*
Polymers / chemistry*
Grant Support
Reg. No./Substance:
0/Peptidomimetics; 0/Polymers; 9001-32-5/Fibrinogen

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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