Understanding the antimicrobial properties/activity of an 11-residue Lys homopeptide by alanine and proline scan.

Amino Acids
Patricio Carvajal-RondanelliFanny Guzmán

Abstract

Previous work demonstrated that lysine homopeptides adopt a polyproline II (PPII) structure. Lysine homopeptides with odd number of residues, especially with 11 residues (K11), were capable of inhibiting the growth of a broader spectrum of bacteria than those with an even number. Confocal studies also determined that K11 was able to localize exclusively in the bacterial membrane, leading to cell death. In this work, the mechanism of action of this peptide was further analyzed focused on examining the structural changes in bacterial membrane induced by K11, and in K11 itself when interacting with bacterial membrane lipids. Moreover, alanine and proline scans were performed for K11 to identify relevant positions in structure conformation and antibacterial activity. To do so, circular dichroism spectroscopy (CD) was conducted in saline phosphate buffer (PBS) and in lipidic vesicles, using large unilamellar vesicles (LUV), composed of 2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) or bacterial membrane lipid. Antimicrobial activity of K11 and their analogs was evaluated in Gram-positive and Gram-negative bacterial strains. The scanning electron microscopy (SEM) micrographs of Staphylococcus aureus ATCC 25923 exposed to the Lys h...Continue Reading

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Citations

Nov 30, 2018·International Journal of Molecular Sciences·Thelma A PertinhezAlberto Spisni
Jun 21, 2020·Antibiotics·Muhammad IdreesAyesha Rahman
Jul 23, 2021·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Johana GómezNils Metzler-Nolte
Aug 28, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Fanny GuzmánConstanza Cárdenas

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Methods Mentioned

BETA
confocal microscopy

Software Mentioned

Spectra Manager

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