Abstract

The bovine lactoferricin L6 (RRWQWR) has been previously identified as a novel cell-penetrating peptide (CPP) that is able to efficiently internalize into human cells. L6 interacts with quantum dots (QDs) noncovalently to generate stable L6/QD complexes that enter cells by endocytosis. In this study, we demonstrate a modified L6 (HL6; CHHHHHRRWQWRHHHHHC), in which short polyhistidine peptides are introduced into both flanks of L6, has enhanced cell-penetrating ability in human bronchoalveolar carcinoma A549 cells. The mechanism of cellular uptake of HL6/QD complexes is primarily direct membrane translocation rather than endocytosis. Dimethyl sulfoxide (DMSO), but not pyrenebutyrate (PB), ethanol, oleic acid, or 1,2-benzisothiazol-3(2 H)-one (BIT), slightly enhances HL6-mediated protein transduction efficiency. Neither HL6 nor HL6/QD complexes are cytotoxic to A549 or HeLa cells. These results indicate that HL6 could be a more efficient drug carrier than L6 for biomedical as well as biotechnological applications, and that the function of polyhistidine peptides is critical to CPP-mediated protein transduction.

Department(s)

Biological Sciences

Comments

This work was supported by the Center for Biomedical Science and Engineering at Missouri University of Science and Technology, and the Ministry of Science and Technology, Taiwan (grant number MOST 107-2320-B-259-005-).

International Standard Serial Number (ISSN)

2045-2322

Document Type

Article - Journal

Document Version

Final Version

File Type

text

Language(s)

English

Rights

© 2019 The Authors, All rights reserved.

Creative Commons Licensing

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.

PubMed ID

31253836

Included in

Biology Commons

Share

 
COinS