ArticleInternational journal of molecular sciences2022
Expanding the Landscape of Amino Acid-Rich Antimicrobial Peptides: Definition, Deployment in Nature, Implications for Peptide Design and Therapeutic Potential.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 50 citations in OpenAlex.
- Purification, Characterization, and In Vitro Safety Assessment of the Antimicrobial Peptide SAM-KB40 from Bacillus licheniformis SAM-D318.Applied biochemistry and biotechnology · 2026Article
- Role of antimicrobial peptide-based biomaterials in respiratory tract infections control.BMC microbiology · 2026Review
- Redefining Therapies for Drug-Resistant Tuberculosis: Synergistic Effects of Antimicrobial Peptides, Nanotechnology, and Computational Design.Advanced healthcare materials · 2026Review
- A Scoping Review of Snail Antibacterial Peptides and Proteins: From Natural Defence to Translational Prospects.Probiotics and antimicrobial proteins · 2026Article
- One-Step Design of Potent and Nonhemolytic Antimicrobial Peptides by Using a Database-Guided, Nonmachine Learning Approach.ACS infectious diseases · 2026Article
- D-amino acid substitution and cyclization enhance the stability and antimicrobial activity of arginine-rich peptides.Microbiology (Reading, England) · 2026Article
- Hybrid and conjugated antimicrobial peptides: new tactics to counter bacterial resistance.Frontiers in microbiology · 2026Review
- Plant Antimicrobial Oligopeptides with Anticancer Properties as a Source of Biologically Active Peptides-AnInternational journal of molecular sciences · 2025Article
- Discovery of a Novel Antimicrobial Peptide fromAntibiotics (Basel, Switzerland) · 2025Article
- A Type Ia Crustin from the Pacific White ShrimpBiomolecules · 2025Article
- The Therapeutic Potential of Antimicrobial Peptides Isolated from the Skin Secretions of Anurans of the GenusToxins · 2025Review
- Cationic antimicrobial peptides: potential templates for anticancer agents.Frontiers in medicine · 2025Review
- Senegalin-2: A Novel Hexadecapeptide fromBiomolecules · 2024Article
- Antimicrobial Peptides from Porcine Blood Cruor Hydrolysates as a Promising Source of Antifungal Activity.Foods (Basel, Switzerland) · 2024Article
- Antimicrobial Peptides: The Game-Changer in the Epic Battle Against Multidrug-Resistant Bacteria.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Computational Prediction and Structural Analysis of α-Hairpinins, a Ubiquitous Family of Antimicrobial Peptides, Using the Cysmotif Searcher Pipeline.Antibiotics (Basel, Switzerland) · 2024Article
- Antioxidant activities of Saudi honey samples related to their content of short peptides.Scientific reports · 2024Article
- Dual-Action Therapeutics: DNA Alkylation and Antimicrobial Peptides for Cancer Therapy.Cancers · 2024Review
- Vesicle protrusion induced by antimicrobial peptides suggests common carpet mechanism for short antimicrobial peptides.Scientific reports · 2024Article
- Physicochemical and sequence determinants of antiviral peptides.Biologia futura · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Unlike the α-helical and β-sheet antimicrobial peptides (AMPs), our knowledge on amino acid-rich AMPs is limited. This article conducts a systematic study of rich AMPs (>25%) from different life kingdoms based on the Antimicrobial Peptide Database (APD) using the program R. Of 3425 peptides, 724 rich AMPs were identified. Rich AMPs are more common in animals and bacteria than in plants. In different animal classes, a unique set of rich AMPs is deployed. While histidine, proline, and arginine-rich AMPs are abundant in mammals, alanine, glycine, and leucine-rich AMPs are common in amphibians. Ten amino acids (Ala, Cys, Gly, His, Ile, Lys, Leu, Pro, Arg, and Val) are frequently observed in rich AMPs, seven (Asp, Glu, Phe, Ser, Thr, Trp, and Tyr) are occasionally observed, and three (Met, Asn, and Gln) were not yet found. Leucine is much more frequent in forming rich AMPs than either valine or isoleucine. To date, no natural AMPs are simultaneously rich in leucine and lysine, while proline, tryptophan, and cysteine-rich peptides can simultaneously be rich in arginine. These findings can be utilized to guide peptide design. Since multiple candidates are potent against antibiotic-resistant bacteria, rich AMPs stand out as promising future antibiotics.
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