ArticleAntimicrobial agents and chemotherapy2004
Role of positional hydrophobicity in the leishmanicidal activity of magainin 2.
Article in Antimicrobial agents and chemotherapy, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 59 citations in OpenAlex.
- Recent Advances in Therapeutic Peptides: Innovations and Applications in Treating Infections and Diseases.ACS omega · 2025Review
- Peptide Dimerization as a Strategy for the Development of Antileishmanial Compounds.Molecules (Basel, Switzerland) · 2024Article
- Anticancer Mechanisms and Potential Anticancer Applications of Antimicrobial Peptides and Their Nano Agents.International journal of nanomedicine · 2024Review
- Development of New Leishmanicidal Compounds via Bioconjugation of Antimicrobial Peptides and Antileishmanial Guanidines.ACS omega · 2023Article
- Neglected Zoonotic Diseases: Advances in the Development of Cell-Penetrating and Antimicrobial Peptides against Leishmaniosis and Chagas Disease.Pathogens (Basel, Switzerland) · 2023Review
- Essential Role of Enzymatic Activity in the Leishmanicidal Mechanism of the Eosinophil Cationic Protein (RNase 3).ACS infectious diseases · 2022Article
- Activity of Anti-Microbial Peptides (AMPs) againstBiomolecules · 2021Review
- Peptides to Tackle Leishmaniasis: Current Status and Future Directions.International journal of molecular sciences · 2021Review
- Phylloseptin-1 is Leishmanicidal for Amastigotes ofInternational journal of environmental research and public health · 2020Article
- Synergistic combination of alkylphosphocholines with peptaibols in targeting Leishmania infantum in vitro.International journal for parasitology. Drugs and drug resistance · 2018Article
- Emerging therapeutic targets for treatment of leishmaniasis.Expert opinion on therapeutic targets · 2018Review
- Mechanisms of action of substituted β-amino alkanols on Leishmania donovani.Antimicrobial agents and chemotherapy · 2015Article
- Deciphering the magainin resistance process of Escherichia coli strains in light of the cytosolic proteome.Antimicrobial agents and chemotherapy · 2012Article
- Effect of BMAP-28 antimicrobial peptides on Leishmania major promastigote and amastigote growth: role of leishmanolysin in parasite survival.PLoS neglected tropical diseases · 2011Article
- Peptide antimicrobial agents.Clinical microbiology reviews · 2006Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The emergence of membrane-active antimicrobial peptides as new alternatives against pathogens with multiantibiotic resistance requires the design of better analogues. Among the different physicochemical parameters involved in the optimization of linear antimicrobial peptides, positional hydrophobicity has recently been incorporated. This takes into consideration the concept of the topological distribution of hydrophobic residues throughout the sequence rather than the classical concept of hydrophobicity as a global parameter of the peptide, calculated as the summation of the individual hydrophobicities of the residues. In order to assess the contribution of this parameter to the leishmanicidal mechanisms of magainin 2 analogues, the activities of two of these analogues, MG-H1 (GIKKFLHIIWKFIKAFVGEIMNS) and MG-H2 (IIKKFLHSIWKFGKAFVGEIMNI), which have similar charges, amino acid compositions, and hydrophobicities but different positional hydrophobicities, against Leishmania donovani promastigotes were assayed (T. Tachi, R. F. Epand, R. M. Epand, and K. Matsuzaki, Biochemistry 41:10723-10731, 2002). The activities were compared with that of the parental peptide, F5W-magainin 2 (GIGKWLHSAKKFGKAFVGEIMNS). The three peptides were active at micromolar concentrations, in the order MG-H2 > MG-H1 > F5W-magainin 2. These activities differ from their hemolytic and bactericidal activities. The results demonstrate that positional hydrophobicity, which reflects the presence of short stretches of sequences rich in hydrophobic amino acids, plays an important role in the activities of leishmanicidal peptides.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.