2024-03-28T22:45:12Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/508542020-10-20T11:19:20Zcom_10261_86com_10261_1col_10261_339
DIGITAL.CSIC
author
Díaz, Dolores
author
García de la Torre, Beatriz
author
Fernández-Reyes, María
author
Rivas, Luis
author
Andreu, David
author
Jiménez-Barbero, Jesús
2011-09-19
Chembiochem 12(14):2177-2183(2011)
1439-4227
http://hdl.handle.net/10261/50854
10.1002/cbic.201100269
1439-7633
The 3D structures of six linear pentadecapeptides derived from the cecropin A–melittin antimicrobial peptide CA(1–7)M(2–9) [KWKLFKKIGAVLKVL-NH2] have been studied. These analogues are modified by ε-NH2 trimethylation of one or more lysine residues and showed variation in both antimicrobial and cytotoxic activities, depending on the number and position of modified lysines. Since it is expected that these peptides will display a strong conformational ordering when in contact with membranes, we have investigated their structure on the basis of the data extracted from NMR experiments performed in membrane-mimetic environments. We show that inclusion of Nε-trimethylated lysine residues induces a certain degree of structural flexibility, while preserving to a variable extent a largely α-helical structure. In addition, peptide orientation with respect to SDS micelles has been explored by detection of the intensity changes of peptide NMR signals upon addition of a paramagnetic probe (Mn2+ ions)
eng
closedAccess
Antimicrobial peptides
Cecropin A
membranes
NMR spectroscopy
trimethyllysine
Structural Framework for the Modulation of the Activity of the Hybrid Antibiotic Peptide Cecropin A-Melittin [CA(1-7)M(2-9)] by N(ε) -Lysine Trimethylation
artículo
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