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Roles of Amphipathicity and Hydrophobicity in the Micelle-Driven Structural Switch of a 14-mer Peptide Core from a Choline-Binding Repeat

Título :
Roles of Amphipathicity and Hydrophobicity in the Micelle-Driven Structural Switch of a 14-mer Peptide Core from a Choline-Binding Repeat
Autor :
Zamora Carreras, Héctor
Maestro García-Donas, Beatriz
Strandberg, Erik
Ulrich, Anne S.
Sanz, Jesús M.
Jiménez, M. Ángeles
Departamento:
Departamentos de la UMH::Bioquímica y Biología Molecular
Fecha de publicación:
2018-03-15
URI :
http://hdl.handle.net/11000/4783
Resumen :
Choline-binding repeats (CBRs) are ubiquitous sequences with a b-hairpin core that are found in the surface proteins of several microorganisms such as S. pneumoniae (pneumococcus). Previous studies on a 14-mer CBR sequence derived from the pneumoccal LytA autolysin (LytA239–252 peptide) have demonstrated a switch behaviour for this peptide, so that it acquires a stable, native-like bhairpin conformation in aqueous solution but is reversibly transformed into an amphipathic a-helix in the presence of detergent micelles. With the aim of understanding the factors responsible for this unusual b-hairpin to a-helix transition, and to specifically assess the role of peptide hydrophobicity and helical amphipathicity in the process, we designed a series of LytA239–252 variants affecting these two parameters and studied their interaction with dodecylphosphocholine (DPC) micelles by solution NMR, circular dichroism and fluorescence spectroscopies. Our results indicate that stabilising cross-strand interactions become essential for b-hairpin stability in the absence of optimal turn sequences. Moreover, both amphipathicity and hydrophobicity display comparable importance for helix stabilisation of CBR-derived peptides in micelles, indicating that these sequences represent a novel class of micelle/membrane-interacting peptides
Área de conocimiento :
Ciencias puras y naturales: Biología: Biología celular y subcelular. Citología
Tipo documento :
application/pdf
Derechos de acceso:
info:eu-repo/semantics/openAccess
DOI :
https://doi.org/ 10.1002/chem.201704802
Aparece en las colecciones:
Instituto de Biología Molecular y Celular



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