凝聚
化学
极性(国际关系)
生物物理学
肽
膜
赖氨酸
纳米技术
相(物质)
氨基酸
天冬氨酸
分子间力
胶体
生物膜
生物相容性材料
组合化学
透明质酸
肽合成
生物化学
细胞
生物细胞
精氨酸
聚电解质
肽序列
模型系统
固相合成
序列(生物学)
作者
Chengying Yin,Cheng Wu,Xinran Yu,Jie Liu,Lantian Ma,Yifeng Zhu,Liangfei Tian
摘要
Peptide-based coacervates demonstrate remarkable potential across interdisciplinary fields of biomedicine and materials science due to their sequence programmability, dynamic self-assembly capability, and exceptional biocompatibility. Despite progress in understanding their phase behavior, the high charge density and complex intermolecular interactions present significant challenges in precisely tailoring their microenvironments and biological functions. In this study, we utilized decapeptide sequences (decaarginine R10, decalysine K10, and decaaspartic acid D10) to explore the impact of substituting aspartic acid (D) with phenylalanine (F) in D10 or lysine (K) with arginine (R) in K10 on the microenvironment of coacervates. The replacement of D with F in the R10/D10 system led to a thermodynamic shift from enthalpy-driven (low F%) to entropy-driven (high F%) phase separation and enhanced phase separation propensity and salt resistance, while reducing internal polarity and molecular mobility. Varying R% in K10/D10 systems demonstrated limited impact on microdroplet viscosity and polarity compared to F% modulation, despite stabilizing droplets at R% ≥ 20%. Neither the D-to-F nor K-to-R substitutions altered the enrichment of biological macromolecules; however, the D-to-F substitution disrupted the secondary structure of double-stranded DNA. Cell coculture experiments confirmed that both R10/(FD)5 and R10/D10 complex coacervate microdroplets adhered to cell membranes rapidly, but R10/D10 exhibited stronger proliferation inhibition. This molecular-level analysis establishes a foundation for connecting the peptide sequence, condensate microenvironments, and biological functions.
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