Post-assembly α-helix to ß-sheet structural transformation within SAF-p1/p2a peptide nanofibers.
Soft Matter
; 14(44): 8986-8996, 2018 Nov 14.
Article
em En
| MEDLINE
| ID: mdl-30375627
ABSTRACT
We report an unanticipated helix-to-sheet structural transformation within an assembly of SAF-p1 and SAF-p2a designer peptides. Solid-state NMR spectroscopic data support the assembled structure that was targeted by rational peptide design:
an α-helical coiled-coil co-assembly of both peptides. Subsequent to assembly, however, the system converts to a ß-sheet structure that continues to exhibit nearest-neighbor interactions between the two peptide components. The structural transition occurs at pH 7.4 and exhibits strongly temperature-dependent kinetics between room temperature (weeks) and 40 °C (minutes). We further observed evidence of reversibility on the timescale of months at 4 °C. The structural conversion from the anticipated structure to an unexpected structure highlights an important aspect to the challenge of designing peptide assemblies. Furthermore, the conformational switching mechanism mediated by a prerequisite α-helical nanostructure represents a previously unknown route for ß-sheet designer peptide assembly.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Nanofibras
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article