Use of Click Chemistry for Obtaining an Antimicrobial Chimeric Peptide Containing the LfcinB and Buforin II Minimal Antimicrobial Motifs

Pineda-Castañeda, Héctor Manuel; Bonilla-Velásquez, Laura; Leal-Castro, Aura Lucía; Fierro-Medina, Ricardo; García‐Castañeda, Javier Eduardo; Rivera‐Monroy, Zuly Jenny

doi:10.1002/slct.201903834

Cited by 8 publications

(8 citation statements)

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“…The multivalent molecules LfcinB (20-25) 2 and LfcinB (20-25) 4 contain the LfcinB (20-25) motif (RRWQWR) and show inhibition activity against E. coli, P. aeruginosa, and S. aureus. Chimeric peptide chimera 3 containing two motifs, namely, the RRWQWR of LfcinB (20-25) and the RLLR of BFII (32-35), shows high antibacterial activity against E. coli ATCC 25922 and S. aureus ATCC 25923 (Vargas-Casanova et al, 2019;Pineda-Castañeda et al, 2020).…”

Section: "Glycine Zipper" Of Gxxxg Motifsmentioning

confidence: 99%

Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields

et al. 2020

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Antimicrobial peptides (AMPs) are a class of small peptides that widely exist in nature and they are an important part of the innate immune system of different organisms. AMPs have a wide range of inhibitory effects against bacteria, fungi, parasites and viruses. The emergence of antibiotic-resistant microorganisms and the increasing of concerns about the use of antibiotics resulted in the development of AMPs, which have a good application prospect in medicine, food, animal husbandry, agriculture and aquaculture. This review introduces the progress of research on AMPs comprehensively and systematically, including their classification, mechanism of action, design methods, environmental factors affecting their activity, application status, prospects in various fields and problems to be solved. The research progress on antivirus peptides, especially anti-coronavirus (COVID-19) peptides, has been introduced given the COVID-19 pandemic worldwide in 2020.

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Section: "Glycine Zipper" Of Gxxxg Motifsmentioning

confidence: 99%

Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields

et al. 2020

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“…The positive side chains of LfcinB interact electrostatically with the negatively‐charged molecules expressed on the bacterial membrane, and then, the hydrophobic residues bind to the bilipid layer, destabilizing the plasma membrane and causing cell lysis or peptide internalization, [8–14] while buforin II (BFII) is an antimicrobial peptide with extensive activity against Gram‐positive and Gram‐negative bacteria as well as fungi. BFII is internalized in the cytoplasm without causing cell lysis and interacts with DNA and RNA by inhibiting cell functions that lead to cell death [15–19] …”

Section: Introductionmentioning

confidence: 99%

Designing Chimeric Peptides: A Powerful Tool for Enhancing Antibacterial Activity

Pineda-Castañeda

Huertas-Ortiz

Leal-Castro

et al. 2021

Chemistry & Biodiversity

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Chimeric peptides containing short sequences derived from bovine Lactoferricin (LfcinB) and Buforin II (BFII) were synthetized using solid‐phase peptide synthesis (SPPS) and characterized via reversed‐phase liquid chromatography and mass spectrometry. The chimeras were obtained with high purity, demonstrating their synthetic viability. The chimeras’ antibacterial activity against Gram‐positive and Gram‐negative strains was evaluated. Our results showed that all the chimeras exhibited greater antibacterial activity against the evaluated strains than the individual sequences, suggesting that chemical binding of short sequences derived from AMPs significantly increased the antibacterial activity. For each strain, the chimera with the best antibacterial activity exerted a bacteriostatic and/or bactericidal effect, which was dependent on the concentration. It was found that: (i) the antibacterial activity of a chimera is mainly influenced by the linked sequences, the palindromic motif RLLRRLLR being the most relevant one; (ii) the inclusion of a spacer between the short sequences did not significantly affect the chimera's synthesis process; however, it enhanced its antibacterial activity against Gram‐negative and Gram‐positive strains; on the other hand, (iii) the replacement of Arg with Lys in the LfcinB or BFII sequences improved the chimeras’ synthesis process without significantly affecting their antibacterial activity. These results illustrate the great importance of the synthesis of chimeric peptides for the generation of promising antibacterial peptides.

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“…11C ). 343 Alkyne- and azide-containing aa were introduced at the N-termini of LFcin B and buforin II, respectively, and the peptides were joined by a CuAAC reaction. Compared to the parent peptides, the resulting chimera showed improved activity against E. coli and S. aureus .…”

Section: Chemical Synthesis Of Ampsmentioning

confidence: 99%

The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions

et al. 2021

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Use of Click Chemistry for Obtaining an Antimicrobial Chimeric Peptide Containing the LfcinB and Buforin II Minimal Antimicrobial Motifs

Abstract: Scheme 1. Copper-catalyzed azide-alkyne cycloaddition of Pra-RRWQWR (1) with Lys(N 3 )-RLLR (2) for obtaining the chimeric peptide (3)

Cited by 8 publications

References 14 publications

Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields

Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields

Designing Chimeric Peptides: A Powerful Tool for Enhancing Antibacterial Activity

The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions

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