Binding of cationic peptides (KX)4K to DPPG bilayers. Increasing the hydrophobicity of the uncharged amino acid X drives formation of membrane bound β-sheets: A DSC and FT-IR study
-
Add time:08/31/2019 Source:sciencedirect.com
The binding of cationic peptides of the sequence (KX)4K to lipid vesicles of negatively charged dipalmitoyl-phosphatidylglycerol (DPPG) was investigated by differential scanning calorimetry (DSC) and temperature dependent Fourier-transformed infrared (FT-IR) spectroscopy. The hydrophobicity of the uncharged amino acid X was changed from G (glycine) over A (alanine), Abu (α-aminobutyric acid), V (valine) to L (leucine). The binding of the peptides caused an increase of the phase transition temperature (Tm) of DPPG by up to 20 °C. The shift depended on the charge ratio and on the hydrophobicity of the amino acid X. Unexpectedly, the upward shift of Tm increased with increasing hydrophobicity of X. FT-IR spectroscopy showed a shift of the CH2 stretching vibrations of DPPG to lower frequency, particularly for bilayers in the liquid-crystalline phase, indicating an ordering of the hydrocarbon chains when the peptides were bound. Changes in the lipid C=O vibrational band indicated a dehydration of the lipid headgroup region after peptide binding. (KG)4K was bound in an unordered structure at all temperatures. All other peptides formed intermolecular antiparallel β-sheets, when bound to gel phase DPPG. However, for (KA)4K and (KAbu)4K, the β-sheets converted into an unordered structure above Tm. In contrast, the β-sheet structures of (KV)4K and (KL)4K remained stable even at 80 °C when bound to the liquid-crystalline phase of DPPG. Strong aggregation of DPPG vesicles occurred after peptide binding. For the aggregates, we suggest a structure, where aggregated single β-sheets are sandwiched between opposing DPPG bilayers with a dehydrated interfacial region.
We also recommend Trading Suppliers and Manufacturers of gamma-poly-alpha,gamma-diaminobutyric acid (cas 117153-91-0). Pls Click Website Link as below: cas 117153-91-0 suppliers
Prev:Induced circular dichroism and structure of the complexes of poly(l-ornithine) and poly(lα,γ-diaminobutyric acid) with azo dyes
Next:Original ArticleAn Amino Acid-based Amphoteric Liposomal Delivery System for Systemic Administration of siRNA) - 【Back】【Close 】【Print】【Add to favorite 】
- Related Information
- Original ArticleAn Amino Acid-based Amphoteric Liposomal Delivery System for Systemic Administration of siRNA09/01/2019
- Induced circular dichroism and structure of the complexes of poly(l-ornithine) and poly(lα,γ-diaminobutyric acid) with azo dyes08/30/2019
- Pharmaceutical NanotechnologySynthesis of a l-lysine-based alternate alpha,epsilon-peptide: A novel linear polycation with nucleic acids-binding ability08/29/2019
- Account/RevueSynthesis, chemistry, physicochemical properties and industrial applications of amino acid surfactants: A review08/28/2019
- PMR studies on the conformation of poly-(N-γ-carbobenzoxy-L-α-γ-diaminobutyric acid)☆08/27/2019
- Syntheses and conformational studies of poly(γ-N-alkyl-l-α,γ-diaminobutyric acids) and their carbobenzoxy derivatives08/26/2019
- Three generations of α,γ-diaminobutyric acid modified poly(propyleneimine) dendrimers and their cisplatin-type platinum complexes08/25/2019


