ArticleInternational journal of molecular sciences2012
Role of helicity on the anticancer mechanism of action of cationic-helical peptides.
Article in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
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Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Roles of d-Amino Acids on the Bioactivity of Host Defense Peptides.International journal of molecular sciences · 2016Pooled it
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- Anti‑angiogenic effect ofInternational journal of oncology · 2025Article
- Exploration of novel cationic amino acid-enriched short peptides: design, SPPS, biological evaluation andRSC advances · 2024Article
- From oncolytic peptides to oncolytic polymers: A new paradigm for oncotherapy.Bioactive materials · 2024Review
- A Pleurocidin-Like Peptide from Poecilia Mexicana Fish Induces Selective Cytotoxicity in Leukemia Jurkat Cells Through The Apoptosis Pathway.Cell journal · 2023Article
- Evaluation of the antitumor activity of moronecidin (Piscidin)-like peptide in combination with anti-PD-1 antibody against melanoma tumor.Iranian journal of basic medical sciences · 2023Article
- Role of Anti-Cancer Peptides as Immunomodulatory Agents: Potential and Design Strategy.Pharmaceutics · 2022Review
- The Influence of Short Motifs on the Anticancer Activity of HB43 Peptide.Pharmaceutics · 2022Article
- Membrane-disruptive peptides/peptidomimetics-based therapeutics: Promising systems to combat bacteria and cancer in the drug-resistant era.Acta pharmaceutica Sinica. B · 2021Review
- Immunogenic Cell Death Inducing Fluorinated Mitochondria-Disrupting Helical Polypeptide Synergizes with PD-L1 Immune Checkpoint Blockade.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Rediscovery of antimicrobial peptides as therapeutic agents.Journal of microbiology (Seoul, Korea) · 2021Review
- CancerGram: An Effective Classifier for Differentiating Anticancer from Antimicrobial Peptides.Pharmaceutics · 2020Article
- Peptides with Dual Antimicrobial-Anticancer Activity: Strategies to Overcome Peptide Limitations and Rational Design of Anticancer Peptides.Molecules (Basel, Switzerland) · 2020Review
- Antimicrobial Peptides: Interaction With Model and Biological Membranes and Synergism With Chemical Antibiotics.Frontiers in chemistry · 2018Review
- Guided Formation of 3D Helical Mesostructures by Mechanical Buckling: Analytical Modeling and Experimental Validation.Advanced functional materials · 2016Article
- Enantiomeric CopA3 dimer peptide suppresses cell viability and tumor xenograft growth of human gastric cancer cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Article
- Tryptophan as a probe to study the anticancer mechanism of action and specificity of α-helical anticancer peptides.Molecules (Basel, Switzerland) · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present study, the 26-residue amphipathic α-helical peptide A12L/A20L (Ac-KWKSFLKTFKSLKKTVLHTLLKAISS-amide) with strong anticancer activity and specificity was used as the framework to study the effects of helicity of α-helical anticancer peptides on biological activities. Helicity was systematically modulated by introducing d-amino acids to replace the original l-amino acids on the non-polar face or the polar face of the helix. Peptide helicity was measured by circular dichroism spectroscopy and was demonstrated to correlate with peptide hydrophobicity and the number of d-amino acid substitutions. Biological studies showed that strong hemolytic activity of peptides generally correlated with high hydrophobicity and helicity. Lower helicity caused the decrease of anti-HeLa activity of peptides. By introducing d-amino acids to replace the original l-amino acids on the non-polar face or the polar face of the helix, we improved the therapeutic index of A12L/A20L against HeLa cells by 9-fold and 22-fold, respectively. These results show that the helicity of anticancer peptides plays a crucial role for biological activities. This specific rational approach of peptide design could be a powerful method to improve the specificity of anticancer peptides as promising therapeutics in clinical practices.
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