Effects of Two Novel Peptides from Skin of Lithobates Catesbeianus on Tumor Cell Morphology and Proliferation

Zhao, Ruili; Han, Junyou; Wang, Han; He, Hongxuan; Ma, Jingyun

doi:10.5772/25209

Cited by 9 publications

(13 citation statements)

References 15 publications

(12 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This resulted in 101 candidate mature sequences, which we fed into AMPlify, predicting 75 of them to be putative AMPs. We selected peptides between five to 35 amino acids in length with a positive charge for further analysis, yielding a final list of 16 peptides (Table 2), five of which were previously reported sequences from literature or AMP databases [28][29][30] . The remaining 11 peptides were synthesized and evaluated in vitro.…”

Section: Amp Discoverymentioning

confidence: 99%

See 1 more Smart Citation

AMPlify: attentive deep learning model for discovery of novel antimicrobial peptides effective against WHO priority pathogens

Sutherland

Hammond

et al. 2020

Preprint

View full text Add to dashboard Cite

Antibiotic resistance is a growing global health concern prompting researchers to seek alternatives to conventional antibiotics. Antimicrobial peptides (AMPs) are emerging therapeutic agents with promising utility in this domain and using in silico methods to discover novel AMPs is a strategy that is gaining interest. Such methods can filter through large volumes of candidate sequences and reduce lab screening costs. Here we introduce AMPlify, an attentive deep learning model for AMP prediction, and demonstrate its utility in prioritizing peptide sequences derived from the Rana [Lithobates] catesbeiana (bullfrog) genome. We tested the bioactivity of our predicted peptides against a panel of bacterial species, including representatives from the World Health Organization’s “priority pathogens” list. Four of our novel AMPs were active against multiple species of bacteria, including a multi-drug resistant isolate of carbapenemase-producing Escherichia coli, demonstrating the utility of tools like AMPlify in our fight against antibiotic resistance.

show abstract

Section: Amp Discoverymentioning

confidence: 99%

“…IB is a co-founder of and executive at Amphoraxe Life Sciences Inc. [28][29][30] . + Previously reported as a full-length AMP precursor sequence.…”

Section: Author Contributionsmentioning

confidence: 99%

AMPlify: attentive deep learning model for discovery of novel antimicrobial peptides effective against WHO priority pathogens

Sutherland

Hammond

et al. 2020

Preprint

View full text Add to dashboard Cite

show abstract

“…In common with other HDPs isolated from frogs belonging to the Ranidae family, it contains a cyclic disulphide bridged domain at the Cterminal end of the peptide sequence, between residues 23 and 29. Palustrin-Ca is biologically interesting, as it non-hemolytic, and exhibits potent broadspectrum antibacterial activity, and as previously mentioned, very potent anticancer activity, with an IC 50 of 0.951 µg/ml against human gastric cancer SGC-7901 [8] . In this work, palustrin-Ca's conformation and structural properties are elucidated using NMR spectroscopy, with an ensemble of model structures being determined.…”

Section: Introductionmentioning

confidence: 74%

“…HDPs have also been demonstrated to possess antifungal, antiparasitic, antiviral and anticancer activities [7] . Indeed, palustrin-Ca (GFLDIIKDTGKEFAVKILNNLKCKLAG-GCPP) is reported to be the most potent known anticancer peptide, with an IC 50 of 0.951 µg/ml against human gastric cancer SGC-7901 [8] .…”

Section: Introductionmentioning

confidence: 99%

“…Our laboratory has conducted structural studies on various amphibian HDPs, including ranatuerin-2CSa [21] , XT-7 [22] , alyteserin-1c [23] , brevinin-1BYa [24] and its analogues [25] , maximin 3 [26] and maximin 1 [27] . Palustrin-Ca (GFLDIIKDTGKEFAVKILNNLKCKLAGGCPP) is a 31 amino acid residue HDP first isolated from the skin of the American bullfrog Lithobates catesbeianus [8] . In common with other HDPs isolated from frogs belonging to the Ranidae family, it contains a cyclic disulphide bridged domain at the Cterminal end of the peptide sequence, between residues 23 and 29.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca

Timmons

Hewage

2021

Preprint

View full text Add to dashboard Cite

Palustrin-Ca (GFLDIIKDTGKEFAVKILNNLKCKLAGGCPP) is a host defense peptide with potent antimicrobial and anticancer activities, first isolated from the skin of the American bullfrog Lithobates catesbeianus. The peptide is 31 amino acid residues long, cationic and amphipathic. Two-dimensional NMR spectroscopy was employed to characterise its three-dimensional structure in a 50/50% water/2,2,2-trifluoroethanol-d3 mixture. The structure is defined by an α-helix that spans between Ile6-Ala26, and a cyclic disulphide bridged domain at the C-terminal end of the peptide sequence, between residues 23 and 29. A molecular dynamics simulation was employed to model the peptide's interactions with sodium dodecyl sulphate micelles, a widely used bacterial membrane-mimicking environment. Throughout the simulation, the peptide was found to maintain its α-helical conformation between residues Ile6-Ala26, while adopting a position parallel to the surface to micelle, which is energetically-favourable due to many hydrophobic and electrostatic contacts with the micelle.

show abstract

A Comprehensive Review of Patented Antimicrobial Peptides from Amphibian Anurans

García,

Fuentes,

Alonso

et al. 2024

J. Nat. Prod.

View full text Add to dashboard Cite

Since the 1980s, studies of antimicrobial peptides (AMPs) derived from anuran skin secretions have unveiled remarkable structural diversity and a wide range of activities. This study explores the potential of these peptides for drug development by examining granted patents, amino acid modifications related to patented peptides, and recent amphibians' taxonomic updates influencing AMP names. A total of 188 granted patents related to different anuran peptides were found, with Asia and North America being the predominant regions, contributing 65.4% and 15.4%, respectively. Conversely, although the Neotropical region is the world's most diversified region for amphibians, it holds only 3.7% of the identified patents. The antimicrobial activities of the peptides are claimed in 118 of these 188 patents. Additionally, for 160 of these peptides, 66 patents were registered for the natural sequence, 69 for both natural and derivative sequences, and 20 exclusively for sequence derivatives. Notably, common modifications include alterations in the side chains of amino acids and modifications to the peptides' N-and C-termini. This review underscores the biomedical potential of anuran-derived AMPs, emphasizing the need to bridge the gap between AMP description and practical drug development while highlighting the urgency of biodiversity conservation to facilitate biomedical discoveries.

show abstract

Effects of Two Novel Peptides from Skin of Lithobates Catesbeianus on Tumor Cell Morphology and Proliferation

Cited by 9 publications

References 15 publications

AMPlify: attentive deep learning model for discovery of novel antimicrobial peptides effective against WHO priority pathogens

AMPlify: attentive deep learning model for discovery of novel antimicrobial peptides effective against WHO priority pathogens

Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca

A Comprehensive Review of Patented Antimicrobial Peptides from Amphibian Anurans

Contact Info

Product

Resources

About