Structural Characterization of Histatin 5-Spermidine Conjugates: A Combined Experimental and Theoretical Study

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

Histatin 5 (Hst5) is a naturally occurring antimicrobial peptide that acts as the first line of defense against oral candidiasis. It has been shown that conjugation of the active Hst5 fragment, Hst54-15, and the polyamine spermidine (Spd) improves the candidacidal effect. Knowledge about the structure of these conjugates is, however, very limited. Thus, the aim of this study was to characterize the structural properties of the Hst54-15-Spd conjugates by performing atomistic molecular dynamics simulations in combination with small-angle X-ray scattering. It was shown that the Hst54-15-Spd conjugates adopt extended and slightly rigid random coil conformations without any secondary structure in aqueous solution. It is hypothesized that the increased fungal killing potential of Hst54-15-Spd, in comparison with the Spd-Hst54-15 conjugate, is due to the more extended conformations of the former, which cause the bonded Spd molecule to be more accessible for recognition by polyamine transporters in the cell.

Detaljer

Författare
Enheter & grupper
Externa organisationer
  • Temple University
  • University at Buffalo
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Teoretisk kemi
  • Odontologi
Originalspråkengelska
Sidor (från-till)1330-1341
Antal sidor12
TidskriftJournal of Chemical Information and Modeling
Volym57
Utgivningsnummer6
StatusPublished - 2017 jun 26
PublikationskategoriForskning
Peer review utfördJa

Relaterad forskningsoutput

Stephanie Jephthah, 2019 apr 15, Lund: Printed in Sweden by Media-Tryck, Lund University. 94 s.

Forskningsoutput: AvhandlingLicentiatavhandling

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