Arginine-rich peptides vs. lysine-rich peptides: interaction with differently charged lipid bilayers

Jakas, Andreja; Pašalić, Lea; Bakarić, Danijela (2024) Arginine-rich peptides vs. lysine-rich peptides: interaction with differently charged lipid bilayers. In: Journal of peptide science. Prag, Wiley, p. 235 .

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Abstract

Peptides that interact with the cell membrane by disrupting it, by passing through it, or by residing at the membrane interface are known as membrane active peptides. Arginine (Arg or R)- and lysine (Lys or K)-rich cationic peptides are known to have antimicrobial activity, since cationic residues attract the peptide to the anionic bacterial membrane [1]. Arg-rich peptides are more prevalent in natural occurring antimicrobial peptides than Lys, implying that guanidinium group in Arg interacts in different way with biological membranes than the amine group in Lys [2, 3]. As antimicrobial peptides (AMP) have potential application as antibiotics, a better understanding of peptide-lipid interaction is essential to decipher their mechanism of action [4]. In order to get more detailed insight into the interaction of cationic peptides RRRRRFF and KKKKKFF, synthesized by solid phase synthesis, and lipid bilayers prepared from anionic 2-dipalmitoyl-sn- glycero-3-phosphatidylserine (DPPS) lipid and zwitterionic 1, 2- dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), we performed a calorimetric and spectroscopic study. For the purpose of determining the impact of peptides on thermotropic properties lipid bilayers, UV-Vis spectroscopy and differential scanning calorimetry (DSC) have been used, and for molecular- level details of their interaction, FTIR spectroscopy has been used.

Item Type:	Conference or workshop item published in conference proceedings (UNSPECIFIED)
Uncontrolled Keywords:	Liposomes; peptides; biomembranes; calorimetry; spectroscopy
Subjects:	NATURAL SCIENCES NATURAL SCIENCES > Chemistry INTERDISCIPLINARY FIELDS OF ART
Divisions:	Division of Organic Chemistry and Biochemistry
Depositing User:	Kristina Ciglar
Date Deposited:	21 May 2025 12:47
URI:	http://fulir.irb.hr/id/eprint/9818
DOI:	10.17952/37EPS.2024.P1280

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