Biomembrane induced in situ self-assembly of peptide with enhanced antimicrobial activity.,Biomaterials Science

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Biomembrane induced in situ self-assembly of peptide with enhanced antimicrobial activity.
Biomaterials Science ( IF 5.8 ) Pub Date : 2020-02-17 , DOI: 10.1039/c9bm01785b
Zhiwei Shen ₁ , Zhen Guo ₁ , Limin Zhou ₂ , Yujiao Wang ₁ , Jinjin Zhang ₂ , Jun Hu ₂ , Yi Zhang ₂

Affiliation

Antimicrobial peptides (AMPs) as biocides are of great interest because they have the ability to combat antibiotic resistance. Normally, natural AMPs need to be rationally designed or modified for practical use as an antibiotic. Here, a novel AMP, termed FF8, which is a cationic octapeptide composed of arginine, lysine, and phenylalanine, was designed. The FF8 was found to self-assemble into nanofibers when induced by a negatively charged lipid membrane or pH is above 9.4. The fibers on the membrane broke the lipid membrane, forming pores and significantly reducing its fluidity. FF8 also exhibited enhanced antibacterial activity by significantly increasing the permeability of the inner and outer membranes of Escherichia coli (E. coli) and maintaining the pores of the inner membrane of cells, which caused continuous membrane leakage. Because of its high antibacterial activity, cytocompatibility, and cost-effectiveness, FF8 is a promising antibacterial material.

中文翻译：

生物膜诱导的肽原位自组装具有增强的抗菌活性。

作为杀菌剂的抗菌肽（AMPs）具有极大的吸引力，因为它们具有抵抗抗生素耐药性的能力。通常，需要对天然AMP进行合理的设计或修饰，以实际用作抗生素。在这里，设计了一种新型的称为FF8的AMP，它是一种由精氨酸，赖氨酸和苯丙氨酸组成的阳离子八肽。当带负电荷的脂质膜或pH值高于9.4时，发现FF8可自组装成纳米纤维。膜上的纤维会破坏脂质膜，形成孔并显着降低其流动性。FF8还通过显着增加大肠杆菌（E. coli）的内膜和外膜的渗透性并维持细胞内膜的孔而引起了增强的抗菌活性，这导致了连续的膜泄漏。

更新日期：2020-02-17

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