Disulfide engineering on temporin‐<scp>SH</scp>f: Stabilizing the bioactive conformation of an ultra‐short antimicrobial peptide

Dolle, Ashwini; Nagati, Veera Babu; Hunashal, Yamanappa; Krishnamurthy, K. V.; Pasupulati, Anil Kumar; Raghothama, Srinivasarao; Gowd, Konkallu Hanumae

doi:10.1111/cbdd.13525

Cited by 7 publications

(4 citation statements)

References 58 publications

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“…The observed mass of temporin-SHf is consistent with the previous report by Abbassi et al ( 2010 ) on the isolation and characterization of temporin-SHf from the skin secretion of Pelophylax saharica . As reported in our earlier publication (Dolle et al 2019 ), ESI–MS/MS of [M + 2H] 2+ ion of temporin-SHf confirms the fragment series of b and y ions observed in the fragmentation spectrum of temporin-SHf. The fragments at m / z 295, 442, 798, and 911 correspond to b2, b3, b6, and b7 ions.…”

Section: Resultssupporting

confidence: 88%

“…The four Phe residues in this wild frog peptide are reminiscent of human cathelicidin LL-37 features and are remarkably conserved in temporin-SHf, making it a minimal LL-37-like peptide (Wang et al 2019 ). With the disulfide engineering strategy, hydrophobic residues were mutated with hydrophobic cysteine disulfide to yield designed temporin‐SHf and have a chemical nature to that of native peptide, showing improved stability and antimicrobial activity (Dolle et al 2019 ). Temporin‐SHf is a good model for peptidomimetic studies and for developing viable temporin‐SHf‐based antimicrobial/anticancer drugs.…”

Section: Introductionmentioning

confidence: 99%

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Antimicrobial and antitumor properties of anuran peptide temporin-SHf induce apoptosis in A549 lung cancer cells

Antony,

Purayil,

Olakkaran

et al. 2024

Amino Acids

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Temporin-SHf is a linear, ultra-short, hydrophobic, α-helix, and phe-rich cationic antimicrobial peptide. The antitumor activities and mechanism of temporin-SHf-induced cancer cell death are unknown. The temporin-SHf was synthesized by solid-phase Fmoc chemistry and antimicrobial and antitumor activities were investigated. Temporin-SHf was microbiocidal, non-hemolytic, and cytotoxic to human cancer cells but not to non-tumorigenic cells. It affected the cancer cells' lysosomal integrity and caused cell membrane damage. The temporin-SHf inhibited A549 cancer cell proliferation and migration. It is anti-angiogenic and causes cancer cell death through apoptosis. The molecular mechanism of action of temporin-SHf confirmed that it kills cancer cells by triggering caspase-dependent apoptosis through an intrinsic mitochondrial pathway. Owing to its short length and broad spectrum of antitumor activity, temporin-SHf is a promising candidate for developing a new class of anticancer drugs.

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Section: Resultssupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Antimicrobial and antitumor properties of anuran peptide temporin-SHf induce apoptosis in A549 lung cancer cells

Antony,

Purayil,

Olakkaran

et al. 2024

Amino Acids

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“…Moreover, the qRT-PCR result explained that GERM CLEAN impaired virulence of S. mutans through downregulating expression of EPS-and acid-production related genes. e antibacterial activity of GERM CLEAN was preliminarily verified through the antibacterial ring test, but the diameter of inhibition zones formed by GERM CLEAN was not very stable, which varied from 8.4 mm to 12 mm according to our repeated tests, and we suspected that it might be related to the variety of the peptide stability [64][65][66][67][68][69], and this hypothesis needs further confirmation.…”

Section: Discussionmentioning

confidence: 97%

Antimicrobial Effect of a Peptide Containing Novel Oral Spray on Streptococcus mutans

Xiong

Chen

et al. 2020

BioMed Research International

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Objective. To investigate the antibacterial effect of a novel antimicrobial peptide containing oral spray GERM CLEAN on Streptococcus mutans (S. mutans) in vitro and further explore the related mechanisms at phenotypic and transcriptional levels. Methods. The disk diffusion method was used to preliminarily appraise the antimicrobial effect of GERM CLEAN. The minimal inhibitory concentration (MIC) of GREM CLEAN towards S. mutans was determined by the broth dilution method. S. mutans virulence-related phenotypic assays including initial adhesive assay, pH drop, exopolysaccharides (EPS), and biofilm formation measurements and quantitative real-time PCR (qRT-PCR) were further applied to detect the inhibitory mechanisms of GREM CLEAN at 1/2MIC. Results. The diameter (10.18 ± 1.744 mm) of inhibition zones formed by GERM CLEAN preliminarily indicated its inhibitory effect on the major cariogenic bacteria S. mutans. The minimal inhibitory concentration of GERM CLEAN on S. mutans was 100% mass fraction (the stock solution). The study of the antibacterial mechanism showed that GERM CLEAN had a certain inhibitory effect on the initial adhesion, acid production, extracellular polysaccharides (EPS) production, and biofilm formation of S. mutans. GERM CLEAN disturbed S. mutans biofilm physiology mainly through destruction of biofilm architecture and suppression of bacterial growth. The results of qRT-PCR further confirmed that the expression levels of EPS and lactic acid generation genes including gtfB, gtfC, gtfD, and ldh were significantly repressed by treating with GERM CLEAN, and this was consistent with our phenotypic results. Conclusion. The novel antimicrobial peptide containing oral spray GERM CLEAN has an anti-Streptococcus mutans effect and the inhibitory property may be due to suppression of the virulence factors of S. mutans including adhesive, acidogenicity, EPS, and biofilm formation.

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“…Quantities of the corresponding species were measured by integrating the area under the curve using the protocol provided by Shimadzu Corp. The equilibrium constant ( K eq ) is calculated for the following reactions. , …”

Section: Materials and Methodsmentioning

confidence: 99%

The Redox-Active Conopeptide Derived from the Venom Duct Transcriptome of Conus lividus Assists in the Oxidative Folding of Conotoxin

et al. 2021

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The tetrapeptides Li504 and Li520, differing in the modification of the 4trans-hydroxylation of proline, are novel conopeptides derived from the venom duct transcriptome of the marine cone snail Conus lividus. These predicted mature peptides are homologous to the active site motif of oxidoreductases that catalyze the oxidation, reduction, and rearrangement of disulfide bonds in peptides and proteins. The estimated reduction potential of the disulfide of Li504 and Li520 is within the range of disulfide reduction potentials of oxidoreductases, indicating that they may catalyze the oxidative folding of conotoxins. Conformational features of Li504 and Li520 include the trans configuration of the Cys1−Pro2/Hyp2 peptide bond with a type 1 turn that is similar to the active site motif of glutaredoxin that regulates the oxidation of cysteine thiols to disulfides. Li504-and Li520-assisted oxidative folding of α-conotoxin ImI confirms that Li520 improves the yield of the natively folded peptide by concomitantly decreasing the yield of the non-native disulfide isomer and thus acts as a miniature disulfide isomerase. The geometry of the Cys1−Hyp2 peptide bond of Li520 shifts between the trans and cis configurations in the disulfide form and thiol/thiolate form, which regulates the deprotonation of the N-terminal cysteine residue. Hydrogen bonding of the hydroxyl group of 4-trans-hydroxyproline with the interpeptide chain unit in the mixed disulfide form may play a vital role in shifting the geometry of the Cys1−Hyp2 peptide bond from cis to trans configuration. The Li520 conopeptide together with similar peptides derived from other species may constitute a new family of "redox-active" conopeptides that are integral components of the oxidative folding machinery of conotoxins.

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Disulfide engineering on temporin‐SHf: Stabilizing the bioactive conformation of an ultra‐short antimicrobial peptide

Cited by 7 publications

References 58 publications

Antimicrobial and antitumor properties of anuran peptide temporin-SHf induce apoptosis in A549 lung cancer cells

Antimicrobial and antitumor properties of anuran peptide temporin-SHf induce apoptosis in A549 lung cancer cells

Antimicrobial Effect of a Peptide Containing Novel Oral Spray on Streptococcus mutans

The Redox-Active Conopeptide Derived from the Venom Duct Transcriptome of Conus lividus Assists in the Oxidative Folding of Conotoxin

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