Conformational study of a custom antibacterial peptide cecropin B1: implications of the lytic activity

Srisailam, S; Arunkumar, AI; Wang, W; Yu, C; Chen, HM

HERO ID

5917361

Reference Type

Journal Article

Year

2000

Language

English

PMID

11004545

HERO ID 5917361
In Press No
Year 2000
Title Conformational study of a custom antibacterial peptide cecropin B1: implications of the lytic activity
Authors Srisailam, S; Arunkumar, AI; Wang, W; Yu, C; Chen, HM
Journal Biochimica et Biophysica Acta
Volume 1479
Issue 1-2
Page Numbers 275-285
Abstract Cecropin B1 (CB1) with two amphipathic alpha-helical segments is a derivative of the natural antibacterial peptide, cecropin B. The assays of cell lysis show that, compared with cecropin A (CA), CB1 has a similar ability to lyse bacteria with a higher potency (two- to six-fold higher) in killing cancer cells. The difference may be due to the fact that the peptides possess different structures and sequences. In this study, the solution structure of CB1 in 20% hexafluoroisopropanol was determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The (1)H NMR resonances were assigned. A total of 350 inter-proton distances were used to calculate the solution structure of CB1. The final ensemble structures were well converged, showing the minimum root mean square deviation. The results indicate that CB1 has two stretches of helices spanning from residues 3 to 22 and from residues 26 to 33, which are connected by a hinge section formed by Gly-23 and Pro-24. Lys-25 is partially incorporated in the hinge region. The bent angle between two helical segments located in two planes was between 100 and 110 degrees. With comparisons of the known NMR structure of CA and its activities on bacteria and cancer cells, the structure-function relationship of the peptides is discussed.
Doi 10.1016/S0167-4838(00)00008-X
Pmid 11004545
Wosid WOS:000087933800027
Is Certified Translation No
Dupe Override No
Comments Journal:BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY 0167-4838
Is Public Yes
Language Text English
Keyword nuclear magnetic resonance; conformation; cecropin; lysis