Protective effect of lipidic surfaces against pressure-induced conformational changes of poly(L-lysine)

Download
  1. Get@NRC: Protective effect of lipidic surfaces against pressure-induced conformational changes of poly(L-lysine) (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1021/bi00453a034
AuthorSearch for: ; Search for: ; Search for:
TypeArticle
Journal titleBiochemistry
ISSN0006-2960
1520-4995
Volume29
Issue1
Pages254258
AbstractPoly(L-lysine) bound to phosphatidylglycerol or phosphatidic acid bilayers was submitted to hydrostatic pressure in a diamond anvil cell to investiage whether the lipidic surfaces can protect the polypeptide against pressure-induced conformational transformations. The amide I region of the infrared spectrum of dimyristoylphosphatidic acid bound polylysine shows that most of the polypeptide retains its -sheet structure up to 19 kbar, while it is known to convert entirely to α-helix at ~2 kbar in the absence of the lipid [Carrier, D., Mantsch, H. H., & Wong, P. T. T. (1989) Biopolymers (in press)]. The simultaneous binding of the polypeptidic molecules to two opposing bilayers appears to be required in order to preserve the β-sheet structure at pressures over ~9 kbar: a small proportion of the polypeptide, most likely the molecules at the surface of the aggregated bilayers, was found to convert to unordered and eventually to α-helical conformations in the pressure range 9-19 kbar. The decrease from 1612 to 1606 cm⁻¹ of the frequency of the major β-sheet component of the infrared amide I band as the pressure is raised to 6 kbar indicates a strengthening of the interchain hydrogen bonds. The high-pressure infrared spectra of polylysine bound to dimyristoyl- and dipalmitoylphosphatidylglycerol show that the polypeptide remains α-helical up to ~12 kbar, though the changes in the bandshape indicate an increase in hydrogen bond strength. The formation of a small amount of β-sheet was observed during decompression and is attributed to the effect of dehydration on the polypeptidic molecules located at the surface of the aggregates. This study suggests that lipidic surfaces could be used as cocatalysts, to control and protect the active conformation of enzymatic proteins for operation at elevated hydrostatic pressure.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NRC number30205
NPARC number23001509
Export citationExport as RIS
Report a correctionReport a correction
Record identifier444727fb-d53a-45f3-97d6-e58827d6e444
Record created2017-02-20
Record modified2017-02-20
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)