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Article
Conformational Changes in Pediocin AcH upon Vesicle Binding and Approximation of the Membrane-Bound Structure in Detergent Micelles
Biochemistry
  • Rachel M. Watson, University of Wyoming
  • Robert W. Woody, Colorado State University
  • Randolph V. Lewis, University of Wyoming
  • D. Scott Bohle, University of Wyoming
  • Amy H. Andreotti, Iowa State University
  • Bibek Ray, University of Wyoming
  • Kurt W. Miller, University of Wyoming
Document Type
Article
Publication Version
Published Version
Publication Date
10-1-2001
DOI
10.1021/bi011031p
Abstract
Pediocin AcH is a 44-residue antimicrobial peptide with bactericidal potency against Gram-positive bacteria such as Listeria. It belongs to a family of bacteriocins that, when membrane-associated, is predicted to contain β-sheet and α-helical regions. All bacteriocins in this family have a conserved N-terminal disulfide bond. An additional C-terminal disulfide bond in pediocin AcH is thought to confer enhanced potency and broader specificity range against sensitive bacteria. The C-terminal disulfide bond may also affect the conformation of the C-terminus. The secondary structures of pediocin AcH in aqueous solution and vesicles from susceptible cells, as well as the ability of trifluoroethanol (TFE) and detergent systems to induce secondary structures like those induced in vesicles, were studied by circular dichroism (CD) spectroscopy. Like related peptides, pediocin AcH was highly unordered in aqueous solution, 56%. However, it also contained 20% β-strand and 15% β-turn structures. Upon complete binding to vesicles, 32% α-helical structure formed, the unordered structure decreased to 32%, and the β-strand and β-turn structures remained largely unchanged. Thus, a βα domain structure formed in vesicles. The helical structure likely forces the C-terminal tail to loop back on the helix so that the C24−C44 disulfide bond can form. Detergent micelles were superior to TFE in their ability to induce secondary structural fractions in pediocin AcH comparable to those observed in vesicles. This demonstrates the importance of a hydrocarbon−water interface to pediocin AcH structure induction and suggests that it is preferable to use detergent micelles as solvents in NMR studies of pediocin AcH structure.
Comments

Reprinted (adapted) with permission from Biochemistry 40 (2001): 14037, doi:10.1021/bi011031p. Copyright 2001 American Chemical Society.

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Copyright Owner
American Chemical Society
Language
en
File Format
application/pdf
Citation Information
Rachel M. Watson, Robert W. Woody, Randolph V. Lewis, D. Scott Bohle, et al.. "Conformational Changes in Pediocin AcH upon Vesicle Binding and Approximation of the Membrane-Bound Structure in Detergent Micelles" Biochemistry Vol. 40 Iss. 46 (2001) p. 14037 - 14046
Available at: http://works.bepress.com/amy_andreotti/3/