ArticleThe Journal of biological chemistry2012
Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Antimycobacterial peptides as natural therapeutics for tuberculosis: mechanisms and structural features.Frontiers in antibiotics · 2026Review
- Serendipitous Hinge Modulation Hypothetically Reprograms Caerin 1.1-LC Antibacterial Mechanism and Gram-Negative Selectivity.Pharmaceutics · 2025Article
- The Role of Flexibility in the Bioactivity of Short α-Helical Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2025Review
- Proline-Modified (RW)ACS omega · 2025Article
- Carboxy-Amidated AamAP1-Lys has Superior Conformational Flexibility and Accelerated Killing of Gram-Negative Bacteria.Biochemistry · 2025Article
- Emergent conformational and aggregation properties of synergistic antimicrobial peptide combinations.Nanoscale · 2024Article
- Review
- From oncolytic peptides to oncolytic polymers: A new paradigm for oncotherapy.Bioactive materials · 2024Review
- Antimicrobial Peptides as Immunomodulators and Antimycobacterial Agents to Combat Mycobacterium tuberculosis: a Critical Review.Probiotics and antimicrobial proteins · 2023Review
- Co-Delivery of D-LAK Antimicrobial Peptide and Capreomycin as Inhaled Powder Formulation to Combat Drug-Resistant Tuberculosis.Pharmaceutical research · 2023Article
- Evolutionary andCurrent research in microbial sciences · 2023Article
- Identification and characterization of antimicrobial peptide (AMP) candidate from Gonggong Sea Snail (Journal of food science and technology · 2023Article
- Antimicrobial peptides: A promising tool to combat multidrug resistance in SARS CoV2 era.Microbiological research · 2022Review
- Biophysical Characterization of LTX-315 Anticancer Peptide Interactions with Model Membrane Platforms: Effect of Membrane Surface Charge.International journal of molecular sciences · 2022Article
- Stapling of Peptides Potentiates the Antibiotic Treatment ofAntibiotics (Basel, Switzerland) · 2022Article
- Peptide profiling in cow urine reveals molecular signature of physiology-driven pathways and in-silico predicted bioactive properties.Scientific reports · 2021Article
- Chemical approaches in the development of natural nontoxic peptide Polybia-MP1 as a potential dual antimicrobial and antitumor agent.Amino acids · 2021Review
- Physicochemical Features and Peculiarities of Interaction of AMP with the Membrane.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Antimicrobial Peptides as Potential Anti-Tubercular Leads: A Concise Review.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Molecular Characterization of a Novel Lytic Enzyme LysC fromInternational journal of molecular sciences · 2020Article
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Authors and funding
19 authors.
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Abstract
We used a combination of fluorescence, circular dichroism (CD), and NMR spectroscopies in conjunction with size exclusion chromatography to help rationalize the relative antibacterial, antiplasmodial, and cytotoxic activities of a series of proline-free and proline-containing model antimicrobial peptides (AMPs) in terms of their structural properties. When compared with proline-free analogs, proline-containing peptides had greater activity against Gram-negative bacteria, two mammalian cancer cell lines, and intraerythrocytic Plasmodium falciparum, which they were capable of killing without causing hemolysis. In contrast, incorporation of proline did not have a consistent effect on peptide activity against Mycobacterium tuberculosis. In membrane-mimicking environments, structures with high α-helix content were adopted by both proline-free and proline-containing peptides. In solution, AMPs generally adopted disordered structures unless their sequences comprised more hydrophobic amino acids or until coordinating phosphate ions were added. Proline-containing peptides resisted ordering induced by either method. The roles of the angle subtended by positively charged amino acids and the positioning of the proline residues were also investigated. Careful positioning of proline residues in AMP sequences is required to enable the peptide to resist ordering and maintain optimal antibacterial activity, whereas varying the angle subtended by positively charged amino acids can attenuate hemolytic potential albeit with a modest reduction in potency. Maintaining conformational flexibility improves AMP potency and selectivity toward bacterial, plasmodial, and cancerous cells while enabling the targeting of intracellular pathogens.
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