| Interaction of bombolitin III with phospholipid monolayers and liposomes and effect on the activity of phospholipase A2. | |
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MedLine Citation:
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PMID: 8204603 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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This study is focused on the characterization of the interaction of the amphiphilic peptide bombolitin III (from the bumblebee Megabombus pennsylvanicus) with phospholipid monolayers and vesicles. It is shown that due to the amphiphilic character of its alpha-helical conformation this water-soluble peptide is able to interact in an ordered fashion with phospholipid organized structures. Depending on the temperature, the subphase, and the particular phosphatidylcholine used, the mixed peptide-phospholipid monolayers can be homogeneous or display phase separation. This behavior was observed by means of the Langmuir film balance technique, coupled with an epifluorescence microscope. In well-defined conditions it is possible to visualize the formation of phase-separated peptide domains at the air-water interface and to study the effect of their presence on the organization of the lipid. The action of phospholipase A2 at the lipid-peptide interface was also followed by means of fluorescence microscopy: some evidence that the enzyme preferentially hydrolyzes the phospholipid that is in contact with the peptide is presented. Furthermore, the presence of bombolitin III in L-alpha-DLPC monolayers causes an increase in the initial speed of degradation with phospholipase A2. These results are in agreement with previous findings that show that the bombolitins are activators in vitro of phospholipase A2. Experiments were also performed with peptide fragments corresponding to the alpha-helical sequences of the protein uteroglobin: despite some amphiphilic character, these peptides do not interact strongly with phospholipid monolayers. Only one of these peptides (corresponding to the helix 4-14 in uteroglobin) is adsorbed in the monolayer in a similar fashion to bombolitin III but does not cause an increase in the activity of phospholipase A2. |
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Authors:
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G Signor; S Mammi; E Peggion; H Ringsdorf; A Wagenknecht |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochemistry Volume: 33 ISSN: 0006-2960 ISO Abbreviation: Biochemistry Publication Date: 1994 May |
Date Detail:
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Created Date: 1994-07-08 Completed Date: 1994-07-08 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 6659-70 Citation Subset: IM |
Affiliation:
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University of Padova, Department of Organic Chemistry, Italy. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Bee Venoms / metabolism* Circular Dichroism Hymenoptera Liposomes* Microscopy, Fluorescence Molecular Sequence Data Peptides / metabolism* Phospholipases A / metabolism* Phospholipases A2 Phospholipids / metabolism* Protein Conformation Uteroglobin / chemistry |
| Chemical | |
Reg. No./Substance:
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0/Bee Venoms; 0/Liposomes; 0/Peptides; 0/Phospholipids; 0/bombolitins; 9060-09-7/Uteroglobin; EC 3.1.1.-/Phospholipases A; EC 3.1.1.4/Phospholipases A2 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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