The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Melittin Interaction with Sulfated Cell Surface Sugars
Abstract
Melittin is a 26-residue cationic peptide with cytolytic and antimicrobial properties. Studies on the action mechanism of melittin have focused almost exclusively on the membrane-perturbing properties of this peptide, investigating in detail the melittin-lipid interaction. Here, we report physical-chemical studies on an alternative mechanism by which melittin could interact with the cell membrane. As the outer surface of many cells is decorated with anionic (sulfated) glycosaminoglycans (GAGs), a strong Coulombic interaction between the two oppositely charged molecules can be envisaged. Indeed, the present study using isothermal titration calorimetry reveals a high affinity of melittin for several GAGs, that is, heparan sulfate (HS), dermatan sulfate, and heparin. The microscopic binding constant of melittin for HS is 2.4 x 10 (5) M (-1), the reaction enthalpy is Delta H melittin (0) = -1.50 kcal/mol, and the peptide-to-HS stoichiometry is approximately 11 at 10 mM Tris, 100 mM NaCl at pH 7.4 and 28 degrees C. Delta H melittin (0) is characterized by a molar heat capacity of Delta C P (0) = -227 cal mol (-1) K (-1). The large negative heat capacity change indicates that hydrophobic interactions must also be involved in the binding of melittin to HS. Circular dichroism spectroscopy demonstrates that the binding of the peptide to HS induces a conformational change to a predominantly alpha-helical structure. A model for the melittin-HS complex is presented. Melittin binding was compared with that of magainin 2 and nisin Z to HS. Magainin 2 is known for its antimicrobial properties, but it does not cause lysis of the eukaryotic cells. Nisin Z shows activity against various Gram-positive bacteria. Isothermal titration calorimetry demonstrates that magainin 2 and nisin Z do not bind to HS (5-50 degrees C, 10 mM Tris, and 100 mM NaCl at pH 7.4).
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“analysis of the dependence of affinity constants on sodium chloride concentration (53, 54) indicated that the numbers of purely ionic interactions involved in the HS binding of apoE4 is about 3-fold larger than that for apoE3 (data not shown).”
From Role of the N- and C-Terminal Domains in Binding of Apolipoprotein E Isoforms to Heparan Sulfate and Dermatan Sulfate: A Surface Plasmon Resonance Study (2008) · cites this paper as [54]
Citations
Cites
Manning, G. S. (1978) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500002031 · Cited by 2,941
Zasloff, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5449 · Cited by 2,305
Record, M. T., Anderson, C. F., & Lohman, T. M. (1978) · Quarterly Reviews of Biophysics · doi:10.1017/s003358350000202x · Cited by 1,681
Mode of action of membrane active antimicrobial peptides
Shai, Y. (2002) · Biopolymers · doi:10.1002/bip.10260 · Cited by 1,579
Habermann, E. (1972) · Science · doi:10.1126/science.177.4046.314 · Cited by 1,570
Barrel-Stave Model or Toroidal Model? A Case Study on Melittin Pores
Yang, L., Harroun, T. A., Weiss, T. M., Ding, L., & Huang, H. W. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75802-x · Cited by 1,114
The actions of melittin on membranes
Dempsey, C. E. (1990) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(90)90006-x · Cited by 852
Luo, P., & Baldwin, R. L. (1997) · Biochemistry · doi:10.1021/bi9707133 · Cited by 643
Detergent-like actions of linear amphipathic cationic antimicrobial peptides
Bechinger, B., & Lohner, K. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.07.001 · Cited by 596
The structure of melittin. II. Interpretation of the structure.
Terwilliger, T. C., & Eisenberg, D. S. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)65098-0 · Cited by 503
Cited by
Sorted by citations
Control of cell selectivity of antimicrobial peptides
Matsuzaki, K. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.09.013 · Cited by 715
On the selectivity and efficacy of defense peptides with respect to cancer cells
Harris, F., Dennison, S. R., Singh, J., & Phoenix, D. A. (2011) · Medicinal Research Reviews · doi:10.1002/med.20252 · Cited by 187
Thermodynamics of Melittin Binding to Lipid Bilayers. Aggregation and Pore Formation
Klocek, G., Schulthess, T., Shai, Y., & Seelig, J. (2009) · Biochemistry · doi:10.1021/bi802127h · Cited by 127
Self-citationMarquette, A., & Bechinger, B. (2018) · Biomolecules · doi:10.3390/biom8020018 · Cited by 129
Thermodynamic Characterization of Acacia Gum−β-Lactoglobulin Complex Coacervation
Aberkane, L., Jasniewski, J., Gaïani, C., Scher, J., & Sanchez, C. (2010) · Langmuir · doi:10.1021/la100705d · Cited by 124
Metadata
- Authors
- Klocek, G., & Seelig, J.
- Affiliations
- University of Basel (CH)
- Corresponding author
- Seelig, Joachim
- ORCID
- Seelig, Joachim
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-01-26
- Volume
- 47
- Issue
- 9
- Pages
- 2841-2849
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1975967141
- Cited by
- 60
- References
- 55
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2022: 1 · 2020: 1 · 2019: 3 · 2018: 7 · 2017: 3 · 2016: 6 · 2015: 1 · 2014: 7 · 2013: 6 · 2012: 3
- FWCI
- 5.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- edoc (University of Basel) (submittedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Health Sciences › Medicine › Pharmacology (medical) › Healthcare and Venom Research
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › thermodynamics and calorimetric analyses
- Keywords
- melittin, heparan sulfate, sulfated glycosaminoglycans, cationic antimicrobial peptides, peptide conformational change, alpha-helix, binding enthalpy, hydrophobic interactions, magainin 2, nisin Z, heparin, dermatan sulfate, cell membrane interaction
- MeSH terms
- Calorimetry, Circular Dichroism, Glycosaminoglycans, Heparan Sulfate, Hydrogen-Ion Concentration, Melitten, Models, Biological, Nisin, Protein Binding, Protein Structure, Secondary
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
