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Cited by 60Antimicrobial Peptides and ActivitiesHealthcare and Venom Researchthermodynamics and calorimetric analyses

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

Klocek, Gabriela, Seelig, Joachim·2008·Biochemistry
DOI 10.1021/bi702258z
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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).

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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
DOI
10.1021/bi702258z
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

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