Enhanced cellular uptake of biotinylated antisense oligonucleotide or peptide mediated by avidin, a cationic protein

FEBS Letters

Pardridge, William M.¹  Boado, Ruben J.¹ 

[1] Department of Medicine, Brain Research Institute, UCLA School of Medicine, Los Angeles, California, 90024-1682, USA

关键词: Drug delivery;    Blood-brain barrier;    Glucose transporter;    Vasopressin;   

DOI  :  10.1016/0014-5793(91)80996-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cellular uptake of a model antisense oligonucleotide complementary to 21 bases of the bovine GLUT-1 glucose transporter mRNA and a model vasopressin peptide that were biotinylated, was markedly stimulated by the presence of avidin, a cationic protein. Conversely, the bacterial homologue of avidin, streptavidin, which is a slightly acidic protein, did not facilitate cellular uptake. The avidin-mediated uptake of biotinylated derivatives was competitively inhibited by another cationic protein, protamine, with a K _i or 5 μg/ml; was saturable, temperature- and time-dependent; and was associated with endocytosis, The use of the avidin-biotin system provides a new approach to increasing the cellular uptake of antisense oligonucleotides or peptides.

【 授权许可】

Unknown