Structure and dynamics of angiotensin (1-7) vasoactive peptide in aqueous solution at the density-functional based tight-binding level

Guilherme Ferreira De Lima, Thomas Heine, Hélio A. Duarte

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Structure and dynamics of heptapeptide Angiotensin (1-7) in aqueous solution have been investigated by means of density-functional based tight-binding molecular dynamics simulations. Solvent-solute interactions have been studied using a hybrid QM/MM method. The backbone of the heptapeptide remains relatively rigid in aqueous solution compared to gas phase. The solvent acts as a cushion, preventing the free motion of the molecule. Tyrosine is the residue which presents the smallest flexibility and the largest number of water molecules in its first solvation shell. This is in good agreement with the previously published NMR results. The intra- and intermolecular hydrogen bridges have been quantified and analyzed in terms of conformation and stability.

Original languageEnglish
Pages (from-to)80-86
Number of pages7
JournalMacromolecular Symposia
Volume254
DOIs
Publication statusPublished - 2007 Sep 11

All Science Journal Classification (ASJC) codes

  • Condensed Matter Physics
  • Organic Chemistry
  • Polymers and Plastics
  • Materials Chemistry

Fingerprint Dive into the research topics of 'Structure and dynamics of angiotensin (1-7) vasoactive peptide in aqueous solution at the density-functional based tight-binding level'. Together they form a unique fingerprint.

  • Cite this