Biological Properties, Current Applications and Potential Therapeautic Applications of Brevinin Peptide Superfamily

Zohrab, Fatemeh; Askarian, Saeedeh; Jalili, Amin; Oskuee, Reza Kazemi

doi:10.1007/s10989-018-9723-8

Cited by 18 publications

(21 citation statements)

References 79 publications

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“…The second quadrant included sequences of two AMP families derived from frog skin secretions; dermaseptins (in lime green) and brevinins (in turquoise) in addition to the four insect bactericidins or cecropin D-like peptides (APD00011, APD00032, APD00033, APD00034—orange circles). Most peptides mentioned above lacked experimental validation against red blood cells, only Brevinin-2-related peptide 63 was mentioned as a low hemolytic peptide (APD00599: consensus class probability of 0.55 and percentile outlier score of 0.23). The third quadrant contained several toad-derived maximins (i.e.…”

Section: Resultsmentioning

confidence: 99%

Machine learning-guided discovery and design of non-hemolytic peptides

Plisson¹,

Ramírez-Sánchez²,

Martínez-Hernández³

2020

Sci Rep

104

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Reducing hurdles to clinical trials without compromising the therapeutic promises of peptide candidates becomes an essential step in peptide-based drug design. Machine-learning models are cost-effective and time-saving strategies used to predict biological activities from primary sequences. Their limitations lie in the diversity of peptide sequences and biological information within these models. Additional outlier detection methods are needed to set the boundaries for reliable predictions; the applicability domain. Antimicrobial peptides (AMPs) constitute an extensive library of peptides offering promising avenues against antibiotic-resistant infections. Most AMPs present in clinical trials are administrated topically due to their hemolytic toxicity. Here we developed machine learning models and outlier detection methods that ensure robust predictions for the discovery of AMPs and the design of novel peptides with reduced hemolytic activity. Our best models, gradient boosting classifiers, predicted the hemolytic nature from any peptide sequence with 95–97% accuracy. Nearly 70% of AMPs were predicted as hemolytic peptides. Applying multivariate outlier detection models, we found that 273 AMPs (~ 9%) could not be predicted reliably. Our combined approach led to the discovery of 34 high-confidence non-hemolytic natural AMPs, the de novo design of 507 non-hemolytic peptides, and the guidelines for non-hemolytic peptide design.

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Section: Resultsmentioning

confidence: 99%

Machine learning-guided discovery and design of non-hemolytic peptides

Plisson¹,

Ramírez-Sánchez²,

Martínez-Hernández³

2020

Sci Rep

104

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“…These bacteria include Candida sp., Acinetobacter baumannii strains, Escherichia coli , Klebsiella pneumonia , and Pseudomonas aeruginosa (Migoń et al 2018 ; Ong et al 2021 ). The current application and potential therapeutic applications of Brevinin had been compiled in Zohrab et al ( 2019 ). Besides antimicrobial properties, Brevinin peptides also promote wound healing, stimulate insulin secretion, and cause dendritic cell maturation (Zohrab et al 2019 ).…”

Section: Discussionmentioning

confidence: 99%

Protein Composition and Biomedical Potential of the Skin Secretion of Hylarana erythraea (Schlegel, 1837) (Anura: Ranidae) from Langkawi Archipelago, Kedah, Peninsular Malaysia

Ong

Ismail

Shahrudin

2021

Int J Pept Res Ther

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The skin secretion of amphibians is known for its high content of bioactive compounds. These bioactive compounds are essential for the advancement of biomedical industries. Four wild green paddy frogs, Hylarana erythraea , were collected from various habitat types within the Langkawi Archipelago. These frogs’ skin secretions were collected, extracted, and analysed for their protein compounds together with biomedical potentials using liquid chromatography–mass spectrometry (LC–MS). The total protein concentration of H. erythraea skin secretions was determined as 0.269 mg/mL. Based on the UniProt (Anura) database, we identified 29 proteins. These proteins were categorised as antimicrobial (AMP) (38%), followed by hormone (17%), enzyme (17%), unreviewed proteins (17%), structural proteins (7%), and regulatory proteins (4%). The AMPs identified were from the family of esculentin-1, esculentin-2, brevinin-1, and frenatin-4, while the hormones belonged to the cholecystokinin group. The enzymes detected were adenylate cyclase 9, the suppressor of tumorigenicity 14 protein homolog, and the HGF activator. The structural proteins belonged to toe pad keratin 2 and Krt5.7 proteins, while the single regulatory protein is CCR4-NOT transcription complex subunit 6-like. These proteins have a wide range of biomedical importance, such as wound healings, facilitate digestions, anti-tumours, and anti-cancer effect.

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“…Novel antimicrobial peptides could be considered as therapeutic agents to solve the complications caused by ongoing diseases and emerging disorders [ 28 ]. The Brevinin family is a group of peptides that have been widely studied [ 7 ] and found to exhibit antimicrobial activity, especially the brevinin-1 subfamily.…”

Section: Discussionmentioning

confidence: 99%

Modification and Targeted Design of N-Terminal Truncates Derived from Brevinin with Improved Therapeutic Efficacy

Chen

et al. 2020

Biology

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Antimicrobial peptides (AMPs) are a class of molecules that play an essential role in innate immune regulation. The Brevinin-1 family are AMPs that show strong pharmacological and antimicrobial potential. A novel peptide, B1A, was designed based on the primary structure of brevinin-1PLb and brevinin-1PLc. Subsequently, a synthesised replicate was subjected to a series of bioassays and was found to display antimicrobial activity. However, it also displayed high levels of haemolysis in a horse red blood cell haemolytic assay, suggesting potential toxicity. Therefore, we rationally designed a number of B1A analogues with aim of retaining antimicrobial activity, lowering toxicity, and to explore the structure–activity relationship of its N-terminus. B1A and its analogues still retained the “Rana Box” and the FLP-motif, which is a feature of this subfamily. However, the introduction of Lys and Trp residues into the peptide sequences revealed that antimicrobial activity of these analogues remained unchanged once the hydrophobicity and the charge reached the threshold. Hence, the idea that the hydrophobicity saturation in different situations is related to antimicrobial activity can be understood via the structure–activity relationship. Meanwhile, it could also be the starting point for the generation of peptides with specific antimicrobial activity.

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Biological Properties, Current Applications and Potential Therapeautic Applications of Brevinin Peptide Superfamily

Cited by 18 publications

References 79 publications

Machine learning-guided discovery and design of non-hemolytic peptides

Machine learning-guided discovery and design of non-hemolytic peptides

Protein Composition and Biomedical Potential of the Skin Secretion of Hylarana erythraea (Schlegel, 1837) (Anura: Ranidae) from Langkawi Archipelago, Kedah, Peninsular Malaysia

Modification and Targeted Design of N-Terminal Truncates Derived from Brevinin with Improved Therapeutic Efficacy

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