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Analysis of peptide design in four‐, five‐, and six‐helix bundle template assembled synthetic protein molecules
Author(s) -
Seo Emily S.,
Sherman John C.
Publication year - 2007
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20791
Subject(s) - helix bundle , chemistry , helix (gastropod) , peptide , bundle , crystallography , circular dichroism , sequence (biology) , stereochemistry , protein structure , biochemistry , materials science , biology , ecology , snail , composite material
Four‐, five‐, and six‐helix bundle template assembled synthetic proteins (TASPs) have been synthesized using disulfide bonds between cavitand templates and peptides, and characterized in terms of stability and structural specificity. The peptide sequence (CGGGEELLKKLEE LLKKG) used was originally designed for a four‐helix bundle. The TASPs were analyzed using CD spectroscopy, chemical denaturation studies, NMR spectroscopy, sedimentation equilibria studies, and hydrophobic dye binding studies to determine the effect of a single peptide sequence when incorporated into bundles with different numbers of helices. If the design was indeed idealized for a four‐helix bundle, then the five‐ and six‐helix bundles should be less stable and manifest lower conformational specificity. The TASPs all demonstrated high stability and cooperative unfolding. However, the four‐helix bundle was found to be significantly more stable and nativelike compared to the five‐ and six‐helix bundles. This suggests that the peptide sequence is specific to the four‐helix bundle, as designed. This result demonstrates the ability to design de novo proteins with specified structure, not just generic stability. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 774–779, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com