7ob2 | pdb_00007ob2
NMR structure of the antimicrobial RiLK1 peptide in SDS micelles
Structural highlights
Publication Abstract from PubMedAntimicrobial peptides (AMPs) represent a skilled class of new antibiotics, due to their broad range of activity, rapid killing, and low bacterial resistance. Many efforts have been made to discover AMPs with improved performances, i.e., high antimicrobial activity, low cytotoxicity against human cells, stability against proteolytic degradation, and low costs of production. In the design of new AMPs, several physicochemical features, such as hydrophobicity, net positive charge, propensity to assume amphipathic conformation, and self-assembling properties, must be considered. Starting from the sequence of the dodecapeptide 1018-K6, we designed a new 10-aminoacid peptide, namely RiLK1, which is highly effective against both fungi and Gram-positive and -negative bacteria at low micromolar concentrations without causing human cell cytotoxicity. In order to find the structural reasons explaining the improved performance of RiLK1 versus 1018-K6, a comparative analysis of the two peptides was carried out with a combination of CD, NMR, and fluorescence spectroscopies, while their self-assembling properties were analyzed by optical and atomic force microscopies. Interestingly, the different spectroscopic and microscopic profiles exhibited by the two peptides, including the propensity of RiLK1 to adopt helix arrangements in contrast to 1018-K6, could explain the improved bactericidal, antifungal, and anti-biofilm activities shown by the new peptide against a panel of food pathogens. Key Physicochemical Determinants in the Antimicrobial Peptide RiLK1 Promote Amphipathic Structures.,Falcigno L, D'Auria G, Palmieri G, Gogliettino M, Agrillo B, Tate R, Dardano P, Nicolais L, Balestrieri M Int J Mol Sci. 2021 Sep 16;22(18). pii: ijms221810011. doi:, 10.3390/ijms221810011. PMID:34576174[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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