Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 115, Issue 12, Pages 3185-3192Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp110543g
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Funding
- Ministry of Education and Science of Poland [N N401 015035]
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The ionophore properties of amphotericin B (AmB) are related to the transport of Na+ and K+ ions across the molecular pores formed by this antibiotic in lipid membranes. In this paper, we present a new, complementary mechanism in which the -COO- group of the antibiotic is involved in the binding process of Na+ and K+ ions. Spectroscopic studies indicate that K+ and Na+ ions play an important role in the AmB aggregation process. Evidence in several spectral regions shows that K+ ions exhibit a stronger ionic binding affinity to the -COO- group relative to Na+. Overall, our findings indicate that monovalent ions can affect the molecular organization of AmB in substantially different ways not previously considered to be significant for their biological action.
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