ArticleInternational journal of molecular sciences2018
Antibacterial Activity and Mechanism of Action of Bovine Lactoferricin Derivatives with Symmetrical Amino Acid Sequences.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Conformational plasticity and truncational effects on bovine lactoferricin: structural determinants of enhanced antimicrobial activity.Frontiers in cellular and infection microbiology · 2026Article
- Bovine lactoferricin exerts antibacterial activity against four Gram-negative pathogenic bacteria by transforming its molecular structure.Frontiers in cellular and infection microbiology · 2025Article
- A review on the screening methods for the discovery of natural antimicrobial peptides.Journal of pharmaceutical analysis · 2025Review
- Changes in Length and Positive Charge of Palindromic Sequence RWQWRWQWR Enhance Cytotoxic Activity against Breast Cancer Cell Lines.ACS omega · 2023Article
- In Vitro Antifungal Activity of Chimeric Peptides Derived from Bovine Lactoferricin and Buforin II againstAntibiotics (Basel, Switzerland) · 2022Article
- Kassporin-KS1: A Novel Pentadecapeptide from the Skin Secretion ofAntibiotics (Basel, Switzerland) · 2022Article
- Secondary Structural Transformation of Bovine Lactoferricin Affects Its Antibacterial Activity.Probiotics and antimicrobial proteins · 2021Article
- Structure-function engineering of novel fish gelatin-derived multifunctional peptides using high-resolution peptidomics and bioinformatics.Scientific reports · 2021Article
- Generation of truncated derivatives throughComputational and structural biotechnology journal · 2021Article
- Lactosmart: A Novel Therapeutic Molecule for Antimicrobial Defense.Frontiers in microbiology · 2021Article
- Antimicrobial Mechanism of pBD2 againstMolecules (Basel, Switzerland) · 2020Article
- Selective cytotoxic effect against the MDA-MB-468 breast cancer cell line of the antibacterial palindromic peptide derived from bovine lactoferricin.RSC advances · 2020Article
- Analogs of Periplanetasin-4 Exhibit Deteriorated Membrane-Targeted Action.Journal of microbiology and biotechnology · 2020Article
- Tridecaptin M, a New Variant Discovered in Mud Bacterium, Shows Activity against Colistin- and Extremely Drug-ResistantAntimicrobial agents and chemotherapy · 2019Article
- Synergistic bactericide and antibiotic effects of dimeric, tetrameric, or palindromic peptides containing the RWQWR motif against Gram-positive and Gram-negative strains.RSC advances · 2019Article
- Characterization of the Bioactivity and Mechanism of Bactenecin Derivatives Against Food-Pathogens.Frontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
In recent years, the overuse of antibiotics has become very serious. Many pathogenic bacteria have become resistant to them, with serious potential health consequences. Thus, it is urgent that we develop new antibiotic drugs. Antimicrobial peptides (AMPs) are important endogenous antibacterial molecules that contribute to immunity. Most have spectral antibacterial properties and do not confer drug resistance. In this paper, an 11-residue peptide (LFcinB18⁻28) with a sequence of KCRRWQWRMKK was modified by amino acid substitution to form a symmetrical amino acid sequence. The antibacterial activities and mechanisms of action of engineered peptides including KW-WK (KWRRWQWRRWK), FP-PF (FPRRWQWRRPF), FW-WF (FWRRWQWRRWF), and KK-KK (KKRRWQWRRKK) were investigated. The four engineered peptides could more effectively inhibit bacteria than the original peptide, LFcinB18⁻28. This suggested that a symmetrical amino acid sequence might enhance the antibacterial activity of AMPs. However, only peptides KW-WK, FP-PF, and KK-KK were safe; FW-WF displayed hemolytic activity. The engineered peptides shared cationic and amphipathic characteristics that facilitated interactions with the anionic microbial membranes, leading to disruption of membrane integrity and permeabilizing microbial membranes, resulting in cell death. Therefore, a symmetrical amino acid sequence and related structural parameters offer an alternative approach to the design of AMPs. This will provide a scientific basis for the design and synthesis of new AMPs.
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Registered trials
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.