Solid-state NMR evidence for ?-hairpin structure within MAX8 designer peptide nanofibers.

ABSTRACT: MAX8, a designer peptide known to undergo self-assembly following changes in temperature, pH, and ionic strength, has demonstrated usefulness for tissue engineering and drug delivery. It is hypothesized that the self-assembled MAX8 nanofiber structure consists of closed ?-hairpins aligned into antiparallel ?-sheets. Here, we report evidence from solid-state NMR spectroscopy that supports the presence of the hypothesized ?-hairpin conformation within the nanofiber structure. Specifically, our (13)C-(13)C two-dimensional exchange data indicate spatial proximity between V3 and K17, and (13)C-(13)C dipolar coupling measurements reveal proximity between the V3 and V18 backbone carbonyls. Moreover, isotopic dilution of labeled MAX8 nanofibers did not result in a loss of the (13)C-(13)C dipolar couplings, showing that these couplings are primarily intramolecular. NMR spectra also indicate the existence of a minor conformation, which is discussed in terms of previously hypothesized nanofiber physical cross-linking and possible nanofiber polymorphism.

SUBMITTER: Leonard SR 

PROVIDER: S-EPMC3699732 | biostudies-other | 2013 Jul

REPOSITORIES: biostudies-other