skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Influence of the Charge State on the Structures and Interactions of Vancomycin Antibiotics with Cell-Wall Analogue Peptides: Experimental and Theoretical Studies

Journal Article · · Chemistry - a European Journal, 15(9):2081-2090

In this study we examined the effect of the charge state on the energetics and dynamics of dissociation of the non-covalent complex between the vancomycin and the cell wall peptide analogue Nα,Nε-diacetyl-L-Lys-D-Ala-D-Ala (V-Ac2KDADA). The binding energies between the vancomycin and the peptide were obtained from the RRKM modeling of the time- and energy resolved surface-induced dissociation (SID) experiments. Our results demonstrate that the stability of the complex toward fragmentation increases in the order: [V+Ac2KDADA+H]+2 < [V+Ac2KDADA+H]+ < [V+Ac2KDADA-H]-. Dissociation of the singly protonated and singly deprotonated complex is characterized by very large entropy effects indicating substantial increase in the conformational flexibility of the resulting products. The experimental threshold energies of 1.75 eV and 1.34 eV obtained for the [V+Ac2KDADA-H]- and [V+Ac2KDADA+H]+ , respectively, are in excellent agreement with the results of density functional theory (DFT) calculations. The increased stability of the deprotonated complex observed experimentally is attributed to the presence of three charged sites in the deprotonated complex as compared to only one charged site in the singly protonated complex. The low binding energy of 0.93 eV obtained for the doubly protonated complex suggests that this ion is destabilized by Coulomb repulsion between the singly protonated vancomycin and the singly protonated peptide comprising the complex.

Research Organization:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC05-76RL01830
OSTI ID:
950176
Report Number(s):
PNNL-SA-62595; 17499a; 19802; KC0302020; TRN: US200910%%110
Journal Information:
Chemistry - a European Journal, 15(9):2081-2090, Vol. 15, Issue 9
Country of Publication:
United States
Language:
English

Similar Records

Experimental and Theoretical Studies of the Structures and Interactions of Vancomycin Antibiotics with Cell Wall Analogues
Journal Article · Wed Oct 01 00:00:00 EDT 2008 · Journal of the American Chemical Society, 130(39):13013-13022 · OSTI ID:950176

Effect of the Basic Residue on the Energetics and Dynamics of Dissociation of Phosphopeptides
Journal Article · Sat Dec 15 00:00:00 EST 2012 · International Journal of Mass Spectrometry, 330-332:295-301 · OSTI ID:950176

Shattering of Peptide Ions on Self-Assembled Monolayer Surfaces.
Journal Article · Wed Feb 12 00:00:00 EST 2003 · Journal of the American Chemical Society · OSTI ID:950176