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Interaction of Cyclic and Linear Labaditin Peptides With Anionic and Zwitterionic Micelles

Interaction of Cyclic and Linear Labaditin Peptides With Anionic and Zwitterionic Micelles

S C Barbosa, E M Cilli, L G Dias, C A Fuzo, L Degrève, R G Stabeli, R Itri, P Ciancaglini

J Colloid Interface Sci. 2015 Jan 15;438:39-46.

PMID: 25454423

Abstract:

Conformational changes of the cyclic (Lo) peptide Labaditin (VWTVWGTIAG) and its linear analogue (L1) promoted by presence of anionic sodium dodecyl sulfate (SDS) and zwitterionic L-α-Lysophosphatidylcholine (LPC) micelles were investigated. Results from λ(max) blue-shift of tryptophan fluorescence emission combined with Stern-Volmer constants values and molecular dynamics (MD) simulations indicated that L1 interacts with SDS micelles to a higher extent than does Lo. Further, the MD simulation demonstrated that both Lo and L1 interact similarly with LPC micelles, being preferentially located at the micelle/water interface. The peptide-micelle interaction elicits conformational changes in the peptides. Lo undergoes limited modifications and presents unordered structure in both LPC and SDS micelles. On the other hand, L1 displays a random-coil structure in aqueous medium, pH 7.0, and it acquires a β-structure upon interaction with SDS and LPC, albeit with structural differences in each medium.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4247421	L-α-Lysophosphatidylcholine			Price

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