Hydrophobicity-tuned anion responsiveness underlies endosomolytic cargo delivery mediated by amphipathic vehicle peptides

• Published in: The Journal of biological chemistry Vol. 297; no. 6; p. 101364
• Main Authors: Chen, Xiaolong, Liu, Hanjie, Li, Ang, Ji, Shuangshuang, Fei, Hao
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.12.2021; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; anion sensitivity; Anions; cationic amphipathic peptides; Cell Membrane - metabolism; conformation; Endosomes - metabolism; endosomolytic delivery; Hydrophobic and Hydrophilic Interactions; hydrophobicity; Peptides - chemistry; Peptides - metabolism; CPP; CMP-Neu5Ac; SAP; LUVs; IgG; conformation; 3Fax-Neu5Ac; NY; CPZ; endosomolytic delivery; FITC; TFE; LAMP-1; LAMP-2; IC50; cationic amphipathic peptides; CLSM; CAPs; DOPC; PSA; PBS; DOPG; anion sensitivity; ANS-Na; LC50; hydrophobicity; EIPA; GRAVY; BafA1; PI; IC20; Gly-lit

Peptide conformation can change subject to environment cues. This concept also applies to many cationic amphipathic peptides (CAPs) known to have cell membrane lytic or penetrative activities. Well-conditioned CAPs can match the properties of the target membrane to support their intended biological...