Orientation of membrane-bound melittin studied by a combination of HPLC and liquid secondary ion mass spectrometry (LSIMS).

Abstract:

:Combining two analytical techniques, HPLC and liquid secondary ion mass spectrometry, the orientation of liposomal membrane-bound melittin was analyzed through its trypsin-digested products. We found that trypsin can access all proteolytic sites of the membrane-bound melittin when the liposomes have no transmembrane potential, whereas the proteolytic site near the N terminus of melittin is blocked when the liposomes have a negative transmembrane potential. The results suggest that the negative transmembrane potential may induce the melittin molecules to insert into the membrane perpendicularly, whereas melittin lies flat on the membrane surface in the absence of a negative potential.

journal_name

IUBMB Life

journal_title

IUBMB life

authors

Niu W,Wu Y,Sui SF

doi

10.1080/152165400300001543

keywords:

subject

Has Abstract

pub_date

2000-09-01 00:00:00

pages

215-9

issue

3

eissn

1521-6543

issn

1521-6551

journal_volume

50

pub_type

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