Modulating the Antimicrobial Activity of Temporin L Through Introduction of Fluorinated Phenylalanine

Setty, Subbaiah Chennam; Horam, Soyar; Pasupuleti, Mukesh; Haq, W.

doi:10.1007/s10989-016-9553-5

Cited by 15 publications

(12 citation statements)

References 47 publications

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“…Halogenation is also related to the specificity of AMPs. The o-fluorine substitution in phenylalanine residues maintains the activity of temporin L on E. coli but leads to the loss of activity on S. aureus and P. aeruginosa (Setty et al, 2017).…”

Section: Halogenationmentioning

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: Halogenationmentioning

confidence: 99%

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

et al. 2020

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“…In a further attempt to optimize the parent sequence, we increased the hydrophobicity even more by introducing fluorinated amino acids. As fluorination was reported to lead to minimal steric alterations 41 , we used the mono-, di-and pentafluorinated phenylalanine variants X 1 -X 3 (Table 1 and Figure 2C and Figure S4) pointing to the high impact of the incorporated fluorinated amino acids. In Table 2 all determined MIC 50 values are listed.…”

Section: Figurementioning

confidence: 99%

Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity

Drexelius

Reinhardt

Grabeck

et al. 2021

Biochemical Journal

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Multidrug resistant (MDR) bacteria have adapted to most clinical antibiotics and are a growing threat to human health. One promising type of candidates for the everlasting demand of new antibiotic compounds constitute antimicrobial peptides (AMPs). These peptides act against different types of microbes by permeabilizing pathogen cell membranes, whereas being harmless to mammalian cells. Contrarily, another class of membrane-active peptides, namely cell-penetrating peptides (CPPs), is known to translocate in eukaryotic cells without substantially affecting the cell membrane. Since CPPs and AMPs share several physicochemical characteristics, we hypothesized if we can rationally direct the activity of a CPP towards antimicrobial activity. Herein, we describe the screening of a synthetic library, based on the CPP sC18, including structure-based design to identify the active residues within a CPP sequence and to discover novel AMPs with high activity. Peptides with increased hydrophobicity were tested against various bacterial strains, and hits were further optimized leading to four generations of peptides, with the last also comprising fluorinated amino acid building blocks. Interestingly, beside strong antibacterial activities, we also detected activity in cancer cells, while non-cancerous cells remained unharmed. The results highlight our new candidates, particularly those from generation 4, as a valuable and promising source for the development of future therapeutics with antibacterial activity and beyond.

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“…Halogenation is also associated with AMP specificity. O-fluorine substitution at phenylalanine residues maintains the activity of Temporin L on E. coli but leads to loss of activity on S. aureus and P. aeruginosa [ 154 ]. In addition, PEGylation and glycosylation of amino acid side chain groups are used to improve the bioavailability of peptides [ 124 , 155 , 156 , 157 , 158 ].…”

Section: Therapeutic Potential Of Ampsmentioning

confidence: 99%

S100 Proteins as Novel Therapeutic Targets in Psoriasis and Other Autoimmune Diseases

Kurpet

Chwatko

2022

Molecules

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Psoriasis is one of the most common inflammatory skin diseases affecting about 1–3% of the population. One of the characteristic abnormalities in psoriasis is the excessive production of antimicrobial peptides and proteins, which play an essential role in the pathogenesis of the disease. Antimicrobial peptides and proteins can be expressed differently in normal and diseased skin, reflecting their usefulness as diagnostic biomarkers. Moreover, due to their very important functions in innate immunity, members of host defense peptides and proteins are currently considered to be promising new therapeutic targets for many inflammatory diseases. Koebnerisin (S100A15) belongs to an S100 family of antimicrobial proteins, which constitute the multigenetic group of calcium-binding proteins involved in ion-dependent cellular functions and regulation of immune mechanisms. S100A15 was first discovered to be overexpressed in ‘koebnerized’ psoriatic skin, indicating its involvement in the disease phenotype and the same promising potential as a new therapeutic target. This review describes the involvement of antimicrobial peptides and proteins in inflammatory diseases’ development and therapy. The discussion focuses on S100 proteins, especially koebnerisin, which may be involved in the underlying mechanism of the Köebner phenomenon in psoriasis, as well as other immune-mediated inflammatory diseases described in the last decade.

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Modulating the Antimicrobial Activity of Temporin L Through Introduction of Fluorinated Phenylalanine

Cited by 15 publications

References 47 publications

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

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

Multistep optimization of a cell-penetrating peptide towards its antimicrobial activity

S100 Proteins as Novel Therapeutic Targets in Psoriasis and Other Autoimmune Diseases

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