Solvent Specified Conformation in Poly(α-l-glutamic acid) Thin Films

The ability to control conformational properties of polypeptides in their films is of considerable interest for many possible applications of these materials. By rational choice of the solvent system for film fabrication, control over the conformation of the main chain, the intermolecular hydrogen b...

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Bibliographic Details
Published in:Biomacromolecules Vol. 5; no. 4; pp. 1214 - 1218
Main Authors: Wu, Xiaodong, Yang, Suizhou, Njus, Jeffrey M, Nagarajan, Ramaswamy, Cholli, Ashok L, Samuelson, Lynne A, Kumar, Jayant
Format: Journal Article
Language:English
Published: Washington, DC American Chemical Society 01-07-2004
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Summary:The ability to control conformational properties of polypeptides in their films is of considerable interest for many possible applications of these materials. By rational choice of the solvent system for film fabrication, control over the conformation of the main chain, the intermolecular hydrogen bonding in the side chain is easily achieved in poly(α-l-glutamic acid) (PLGA) thin films. The spectral data from circular dichromism (CD), FT-IR, and solid state 13C NMR spectroscopies suggest that the β-sheet conformation is dominant in PLGA films cast from trifluoroacetic acid (TFA) solution, whereas the right-handed α-helix is dominant in those cast from pyridine or DMF solution. In comparison with films cast from TFA solutions, the films fabricated from pyridine or DMF solutions exhibit strong intermolecular hydrogen bondings between −COOH groups and have a more ordered arrangement of side chains. Moreover, the extent of α-helix conformation of the PLGA backbone in films cast from pyridine or DMF solution is several times higher than that observed in the PLGA powder precipitated from aqueous solution at pH 4. All spectroscopic studies indicate clearly that the solvents (used for casting these films) play a crucial role in directing the organization of PLGA in these thin films.
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ISSN:1525-7797
1526-4602
DOI:10.1021/bm034540a