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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Interactions of tryptophan-rich cathelicidin antimicrobial peptides with model membranes studied by differential scanning calorimetry.
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Interactions of tryptophan-rich cathelicidin antimicrobial peptides with model membranes studied by differential scanning calorimetry.

机译：通过差示扫描量热法研究富色氨酸的Cathelicidin抗菌肽与模型膜的相互作用。

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摘要

The 13-residue cathelicidins indolicidin and tritrpticin are part of a group of relatively short tryptophan-rich antimicrobial peptides that hold potential as future substitutes for antibiotics. Differential scanning calorimetry (DSC) has been applied here to study the effect of indolicidin and tritrpticin as well as five tritrpticin analogs on the phase transition behaviour of model membranes made up of zwitterionic dimyristoylphosphatidylcholine (DMPC, DMPC/cholesterol) and anionic dimyristoylphosphatidyl glycerol (DMPG) phospholipids. Most of the peptides studied significantly modified the phase transition profile, suggesting the importance of hydrophobic forces for the peptide interactions with the lipid bilayers and their insertion into the bilayer. Indolicidin and tritrpticin are both known to be flexible in aqueous solution, but they adopt turn-turn structures when they bind to and insert in a membrane surface. Pro-to-Ala substitutions in tritrpticin, which result in the formation of a stable alpha-helix in this peptide, lead to a substantial increase in the peptide interactions with both zwitterionic and anionic phospholipid vesicles. In contrast, the substitution of the three Trp residues by Tyr or Phe resulted in a significant decrease of the peptide's interaction with anionic vesicles and virtually eliminated binding of these peptides to the zwitterionic vesicles. An increase of the cationic charge of the peptide induced much smaller changes to the peptide interaction with all lipid systems than substitution of particular amino acids or modification of the peptide conformation. The presence of multiple lipid domains with a non-uniform peptide distribution was noticed. Slow equilibration of the lipid-peptide systems due to peptide redistribution was observed in some cases. Generally good agreement between the present DSC data and peptide antimicrobial activity data was obtained.
机译：13个残基的cathelicidins indolicidin和tritrpticin是一组相对较短的富含色氨酸的抗菌肽的一部分，这些肽具有作为抗生素未来替代品的潜力。此处已使用差示扫描量热法（DSC）来研究吲哚美定和曲美汀以及五个曲美霉素类似物对由两性离子二豆蔻酰磷脂酰胆碱（DMPC，DMPC /胆固醇）和阴离子二甲基豆蔻酰磷脂酰甘油（DMPG）组成的模型膜的相变行为的影响）磷脂。研究的大多数肽显着修饰了相变图谱，表明疏水力对于肽与脂质双层相互作用以及将其插入双层的重要性。众所周知，吲哚美定和三苯乙草胺在水溶液中都是柔性的，但是当它们结合并插入膜表面时，它们采用转弯结构。 Tritrpticin中的Proto-Ala取代会导致在该肽中形成稳定的α-螺旋，从而导致肽与两性离子和阴离子磷脂囊泡的相互作用大大增加。相反，三个Trp残基被Tyr或Phe取代导致该肽与阴离子囊泡的相互作用显着降低，并且实际上消除了这些肽与两性离子囊泡的结合。与特定氨基酸的取代或肽构象的修饰相比，肽阳离子电荷的增加引起与所有脂质系统的肽相互作用的变化小得多。注意到存在具有不均匀的肽分布的多个脂质结构域。在某些情况下，由于肽的重新分布，脂肽系统的平衡缓慢。在当前的DSC数据和肽抗微生物活性数据之间通常获得良好的一致性。

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