New design of helix bundle peptide-polymer conjugates.

Abstract:

:We present a new design of peptide-polymer conjugates where a polymer chain is covalently linked to the side chain of a helix bundle-forming peptide. The effect of conjugated polymer chains on the peptide structure was examined using a de novo designed three-helix bundle and a photoactive four-helix bundle. Upon attachment of poly(ethylene glycol) to the exterior of the coiled-coil helix bundle, the peptide secondary structure was stabilized and the tertiary structure, that is, the coiled-coil helix bundle, was retained. When a heme-binding peptide as an example is used, the new peptide-polymer conjugate architecture also preserves the built-in functionalities within the interior of the helix bundle. It is expected that the conjugated polymer chains act to mediate the interactions between the helix bundle and its external environment. Thus, this new peptide-polymer conjugate design strategy may open new avenues to macroscopically assemble the helix bundles and may enable them to function in nonbiological environments.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Shu JY,Tan C,DeGrado WF,Xu T

doi

10.1021/bm800113g

subject

Has Abstract

pub_date

2008-08-01 00:00:00

pages

2111-7

issue

8

eissn

1525-7797

issn

1526-4602

journal_volume

9

pub_type

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