The unusual conformation of cross‐strand disulfide bonds is critical to the stability of β‐hairpin peptides

Abstract

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Structure Elucidation and Functional Studies of a Novel β-hairpin Antimicrobial Peptide from the Marine Polychaeta Capitella teleta

“…Notably, the increase in the intensity was also observed in the presence of POPG or POPC lipids [19]. Gomesin is known as non-dimerizing 18-residue peptide with highly rigid structure stabilized with two disulfide bridges and the flexible Arg-Gly-Arg C-termini [20].…”

“…The bacterial clinical isolates of Gram-negative bacteria (Escherichia coli, Enterobacter cloacae, Acinetobacter baumanii, Klebsiella pneumoniae, Pseudomonas aeruginosa, Serratia marcescens) were collected and provided by Solixant LLC (Solixant LLC, Moscow, Russia) and Sechenov First Moscow State Medical University hospital. The strains were characterized in our previous studies [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34]. Other strains were obtained from American Type Culture Collection (ATCC, Manassas, VA, USA).…”

Unlocking the Potential of the Antimicrobial Peptide Gomesin: From Discovery and Structure–Activity Relationships to Therapeutic Applications

“…Figure 4 shows a comparison of Gm with antimicrobial peptides from other arthropods (e.g., tachyplesin-Ⅰ [ 35 , 36 ], polyphemusin-II [ 37 ], androctonin [ 38 ]) and porcine leukocyte families (e.g., protegrin-Ⅰ [ 39 ]) and reveals high sequence and structural similarity. These peptides all comprise antiparallel β-sheets which contribute to their high stability profiles [ 40 ]. It is noteworthy that the N- and C-termini of these peptides are close to each other, leading to the possibility that they could be joined chemically to produce cyclic derivatives, as described later in this article.…”

The function of peptide-mimetic anionic groups and salt bridges in the antimicrobial activity and conformation of cationic amphiphilic copolymers

“…6,35 For example, the disulde bond (S-S) covalently crosslinks peptide sequences, which stabilizes the conformation of defensins. [36][37][38] Tryptophan residues of antimicrobial peptides are known to penetrate into the interfacial region of lipid bilayers. [39][40][41] Arginine residues form a cation-p complex with tryptophan residues, which facilitates penetration of arginine into the hydrophobic domain of a lipid bilayer.…”