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Literature DB >> 19431595

Does dimeric melittin occur in aqueous solutions?

Abstract

Melittin, a peptide from bee venom, is known to undergo a monomer / tetramer conversion in aqueous solutions. We have studied the possible participation of dimers in the association equilibrium of melittin by sedimentation equilibrium experiments in the analytical ultracentrifuge and subsequent mathematical analysis of the concentration distributions obtained. It was found that the dimeric state is not significantly populated, the contribution of dimer to the total peptide weight probably being below 0.5%.

Year: 1985 PMID： 19431595 PMCID： PMC1329324 DOI： 10.1016/S0006-3495(85)83786-3

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

17 in total

1. Self-association of apo-C-I from the human high density lipoprotein complex.

Authors: J C Osborne; T J Bronzert; H B Brewer
Journal: J Biol Chem Date: 1977-08-25 Impact factor: 5.157

2. Effect of pressure and ionic strength on the self-association of Apo-A-I from the human high density lipoprotein complex.

Authors: S Formisano; H B Brewer; J C Osborne
Journal: J Biol Chem Date: 1978-01-25 Impact factor: 5.157

3. The self-association of melittin and its binding to lipids: an intrinsic fluorescence polarization study.

Authors: J F Faucon; J Dufourcq; C Lussan
Journal: FEBS Lett Date: 1979-06-01 Impact factor: 4.124

4. Conformational change and self association of monomeric melittin.

Authors: J C Talbot; J Dufourcq; J de Bony; J F Faucon; C Lussan
Journal: FEBS Lett Date: 1979-06-01 Impact factor: 4.124

5. The nature of the stable noncovalent dimers of band 3 protein from erythrocyte membranes in solutions of Triton X-100.

Authors: D Schubert; K Boss; H J Dorst; J Flossdorf; G Pappert
Journal: FEBS Lett Date: 1983-10-31 Impact factor: 4.124

Does dimeric melittin occur in aqueous solutions?

1. Self-association of apo-C-I from the human high density lipoprotein complex.

2. Effect of pressure and ionic strength on the self-association of Apo-A-I from the human high density lipoprotein complex.

3. The self-association of melittin and its binding to lipids: an intrinsic fluorescence polarization study.

4. Conformational change and self association of monomeric melittin.

5. The nature of the stable noncovalent dimers of band 3 protein from erythrocyte membranes in solutions of Triton X-100.

6. The sting. Melittin forms channels in lipid bilayers.

7. Effect of pressure on the self-association of melittin.

8. An ultracentrifuge study on the self-association of glucose dehydrogenase from Bacillus megaterium.

9. Physicochemical studies of the protein-lipid interactions in melittin-containing micelles.

10. Self-association of band-protein from human erythrocyte membranes in aqueous solutions.

1. NMR studies on the monomer-tetramer transition of melittin in an aqueous solution at high and low temperatures.