ArticleBiochemistry2012
NMR solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Structure-Antimicrobial Activity Relationships of Recombinant Host Defence Peptides Against Drug-Resistant Bacteria.Microbial biotechnology · 2025Article
- Evaluating Host Defense Peptides: A Comparative Analysis of Synthetic Peptides and Recombinant Concatemers.Biomolecules · 2025Article
- Antimicrobial peptides: natural templates for next-generation therapeutics against antimicrobial resistance.Frontiers in cellular and infection microbiology · 2025Review
- Evaluation of the Binding Mechanism of Human Defensin 5 in a Bacterial Membrane: A Simulation Study.International journal of molecular sciences · 2021Article
- Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins.Journal of visualized experiments : JoVE · 2021Article
- The penetration of human defensin 5 (HD5) through bacterial outer membrane: simulation studies.Journal of molecular modeling · 2021Article
- The function of peptide-mimetic anionic groups and salt bridges in the antimicrobial activity and conformation of cationic amphiphilic copolymers.RSC advances · 2021Article
- Integrated solid-state NMR and molecular dynamics modeling determines membrane insertion of human β-defensin analog.Communications biology · 2019Article
- The adsorption of human defensin 5 on bacterial membranes: simulation studies.Journal of molecular modeling · 2018Article
- Membrane Active Peptides and Their Biophysical Characterization.Biomolecules · 2018Review
- Article
- Structural features of many circular and leaderless bacteriocins are similar to those in saposins and saposin-like peptides.MedChemComm · 2017Review
- Defensins, lectins, mucins, and secretory immunoglobulin A: microbe-binding biomolecules that contribute to mucosal immunity in the human gut.Critical reviews in biochemistry and molecular biology · 2017Review
- Variations in the interaction of human defensins with Escherichia coli: Possible implications in bacterial killing.PloS one · 2017Article
- Proteolysis Triggers Self-Assembly and Unmasks Innate Immune Function of a Human α-Defensin Peptide.Chemical science · 2016Article
- Calcium-induced Tetramerization and Zinc Chelation Shield Human Calprotectin from Degradation by Host and Bacterial Extracellular Proteases.Chemical science · 2016Article
- Conformational landscape and pathway of disulfide bond reduction of human alpha defensin.Protein science : a publication of the Protein Society · 2015Article
- Peptides and Peptidomimetics for Antimicrobial Drug Design.Pharmaceuticals (Basel, Switzerland) · 2015Review
- The Tomato Defensin TPP3 Binds Phosphatidylinositol (4,5)-Bisphosphate via a Conserved Dimeric Cationic Grip Conformation To Mediate Cell Lysis.Molecular and cellular biology · 2015Article
- Visualizing attack of Escherichia coli by the antimicrobial peptide human defensin 5.Biochemistry · 2015Article
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7 authors.
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Abstract
Human defensin 5 (HD5) is a 32-residue host-defense peptide expressed in the gastrointestinal, reproductive, and urinary tracts that has antimicrobial activity. It exhibits six cysteine residues that are regiospecifically oxidized to form three disulfide bonds (Cys(3)-Cys(31), Cys(5)-Cys(20), and Cys(10)-Cys(30)) in the oxidized form (HD5(ox)). To probe the solution structure and oligomerization properties of HD5(ox), and select mutant peptides lacking one or more disulfide bonds, NMR solution studies and analytical ultracentrifugation experiments are reported in addition to in vitro peptide stability assays. The NMR solution structure of HD5(ox), solved at pH 4.0 in 90:10 H(2)O/D(2)O, is presented (PDB: 2LXZ ). Relaxation T(1)/T(2) measurements and the rotational correlation time (τ(c)) estimated from a (15)N-TRACT experiment demonstrate that HD5(ox) is dimeric under these experimental conditions. Exchange broadening of the Hα signals in the NMR spectra suggests that residues 19-21 (Val(19)-Cys(20)-Glu(21)) contribute to the dimer interface in solution. Exchange broadening is also observed for residues 7-14 comprising the loop. Sedimentation velocity and equilibrium studies conducted in buffered aqueous solution reveal that the oligomerization state of HD5(ox) is pH-dependent. Sedimentation coefficients of ca. 1.8 S and a molecular weight of 14 363 Da were determined for HD5(ox) at pH 7.0, supporting a tetrameric form ([HD5(ox)] ≥ 30 μM). At pH 2.0, a sedimentation coefficient of ca. 1.0 S and a molecular weight of 7079 Da, corresponding to a HD5(ox) dimer, were obtained. Millimolar concentrations of NaCl, CaCl(2), and MgCl(2) have a negligible effect on the HD5(ox) sedimentation coefficients in buffered aqueous solution at neutral pH. Removal of a single disulfide bond results in a loss of peptide fold and quaternary structure. These biophysical investigations highlight the dynamic and environmentally sensitive behavior of HD5(ox) in solution, and provide important insights into HD5(ox) structure/activity relationships and the requirements for antimicrobial action.
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