<br>揭示阳离子肽对囊泡结构的影响：深入了解肽-膜相互作用,ACS Applied Bio Materials

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揭示阳离子肽对囊泡结构的影响：深入了解肽-膜相互作用
ACS Applied Bio Materials ( IF 4.6 ) Pub Date : 2023-12-20 , DOI: 10.1021/acsabm.3c00824
Rebecca Alfred ₁ , Gary Bryant ₂ , Jitendra P Mata _{3,

4} , Mrinal Bhave ₁ , Rohan M Shah ₁

Affiliation

抗菌药物耐药性是一个紧迫的全球健康问题，到 2050 年，数百万人的生命将面临风险，因此需要开发具有广谱活性的抗病原微生物替代品。抗菌肽通过对抗微生物、调节免疫力以及通过膜和细胞内靶向减少耐药性的发展，提供了一种有前途的解决方案。 PuroA 是一种源自嘌呤吲哚啉 A 富含色氨酸结构域的合成肽，对多种病原体表现出有效的抗菌活性，而合理设计的 P1 肽因其特定的组成而表现出增强的抗菌活性。本文研究了这些阳离子肽对代表强阴性细菌细胞膜（S-囊泡）、弱阴性细菌细胞膜（W-囊泡）和哺乳动物细胞膜（M-囊泡）的不同类型囊泡的浓度依赖性影响）。为了研究肽和囊泡之间的相互作用，进行了小角度中子散射实验。阳离子肽 PuroA 和 P1 通过静电相互作用与 S 囊泡相互作用，从而产生独特的效果。 PuroA 积聚在囊泡表面，增加R _core和R _Total ，与地毯模型一致。 P1 在较高浓度下会破坏囊泡结构，与去污剂模型一致。这两种肽都不显着影响 W 囊泡，强调了电荷的作用。在不带电的 M 囊泡中，两种肽都会减少R _core和R _Total并增加t _shell ，表明肽插入并改变了双层特性。这些发现为肽-膜相互作用及其对囊泡结构的影响提供了有价值的见解。此外，这些发现的影响延伸到专门针对细菌和哺乳动物细胞膜的创新抗菌剂和药物输送系统的潜在开发。这项研究有助于增进对肽-膜相互作用的理解，并为各种生物医学应用中靶向膜的方法的设计奠定了基础。

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Unraveling the Effects of Cationic Peptides on Vesicle Structures: Insights into Peptide–Membrane Interactions

Antimicrobial resistance is a pressing global health issue, with millions of lives at risk by 2050, necessitating the development of alternatives with broad-spectrum activity against pathogenic microbes. Antimicrobial peptides provide a promising solution by combating microbes, modulating immunity, and reducing resistance development through membrane and intracellular targeting. PuroA, a synthetic peptide derived from the tryptophan-rich domain of puroindoline A, exhibits potent antimicrobial activity against various pathogens, while the rationally designed P1 peptide demonstrates enhanced antimicrobial activity with its specific composition. This paper investigates the concentration-dependent effects of these cationic peptides on distinct types of vesicles representing strong-negative bacterial cell membranes (S-vesicles), weak-negative bacterial cell membranes (W-vesicles), and mammalian cell membranes (M-vesicles). To investigate the interactions between the peptides and vesicles, small-angle neutron scattering experiments were conducted. The cationic peptides, PuroA and P1, interact with S-vesicles through electrostatic interactions, leading to distinct effects. PuroA accumulates on the vesicle surface, increasing R_core and R_total, aligning with the carpet model. P1 disrupts the vesicle structure at higher concentrations, consistent with the detergent model. Neither peptide significantly affects W-vesicles, emphasizing the role of charge. In uncharged M-vesicles, both peptides decrease R_core and R_total and increase t_shell, indicating peptide insertion and altered bilayer properties. These findings provide valuable insights into peptide–membrane interactions and their impact on vesicle structures. Furthermore, the implications of these findings extend to the potential development of innovative antimicrobial agents and drug delivery systems that specifically target bacterial and mammalian membranes. This research contributes to the advancement of understanding peptide–membrane interactions and lays the foundation for the design of approaches for targeting membranes in various biomedical applications.

更新日期：2023-12-20

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