Literature DB >> 15638800

Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion?

Sarah R Dennison1, Frederick Harris, David A Phoenix.   

Abstract

Oblique orientated alpha-helices are highly specialised protein structural elements that penetrate membranes at a shallow angle and are used to promote membrane destabilisation by a number of protein classes. Here, the use of extended hydrophobic moment methodology shows that the amphibian extrudates, aurein 1.2 and citropin 1.1, may use oblique orientated alpha-helices in their antimicrobial action and that such use may be shared by other antimicrobial peptides. This appears to be the first systematic analysis of these peptides for the possession of oblique orientated alpha-helical structure.

Mesh:

Substances:

Year:  2005        PMID: 15638800     DOI: 10.2174/0929866053406039

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  8 in total

1.  Identification and in silico analysis of helical lipid binding regions in proteins belonging to the amphitropic protein family.

Authors:  Rob C A Keller
Journal:  J Biosci       Date:  2014-12       Impact factor: 1.826

2.  Effect of salt on the interaction of Hal18 with lipid membranes.

Authors:  Sarah R Dennison; Adam J Phoenix; David A Phoenix
Journal:  Eur Biophys J       Date:  2012-08-15       Impact factor: 1.733

3.  A theoretical analysis of secondary structural characteristics of anticancer peptides.

Authors:  Sarah R Dennison; Frederick Harris; Tailap Bhatt; Jaipaul Singh; David A Phoenix
Journal:  Mol Cell Biochem       Date:  2009-07-21       Impact factor: 3.396

4.  Investigations into the ability of the peptide, HAL18, to interact with bacterial membranes.

Authors:  Sarah R Dennison; Young Soo Kim; Hyung Joon Cha; David A Phoenix
Journal:  Eur Biophys J       Date:  2008-07-04       Impact factor: 1.733

5.  New user-friendly approach to obtain an Eisenberg plot and its use as a practical tool in protein sequence analysis.

Authors:  Rob C A Keller
Journal:  Int J Mol Sci       Date:  2011-08-30       Impact factor: 5.923

6.  Penetration of milk-derived antimicrobial peptides into phospholipid monolayers as model biomembranes.

Authors:  Wanda Barzyk; Ewa Rogalska; Katarzyna Więcław-Czapla
Journal:  Biochem Res Int       Date:  2013-12-17

Review 7.  Plant antimicrobial peptides: structures, functions, and applications.

Authors:  Junpeng Li; Shuping Hu; Wei Jian; Chengjian Xie; Xingyong Yang
Journal:  Bot Stud       Date:  2021-04-29       Impact factor: 2.787

8.  Morphing of Amphipathic Helices to Explore the Activity and Selectivity of Membranolytic Antimicrobial Peptides.

Authors:  Alex T Müller; Gernot Posselt; Gisela Gabernet; Claudia Neuhaus; Simon Bachler; Markus Blatter; Bernhard Pfeiffer; Jan A Hiss; Petra S Dittrich; Karl-Heinz Altmann; Silja Wessler; Gisbert Schneider
Journal:  Biochemistry       Date:  2020-09-16       Impact factor: 3.162

  8 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.