Engineering S-protein fragments of bovine ribonuclease A for targeted drug delivery.

Abstract:

:High affinity interaction between S-protein and S-peptide fragments of bovine pancreatic RNase A has been recently used for construction of molecular vehicles for targeted drug delivery. The vehicle is assembled as a complex of drug carrier conjugated S-protein with S-peptide-tagged targeting protein. To avoid random chemical crosslinking of drug carriers to S-protein, we constructed a mutant 16-124aa fragment of RNase A in which 122ala is replaced with a cysteine residue. The mutant and the corresponding wild type fragments expressed in Escherichia coli are refolded into functional conformations only in the presence of S-peptide. After the removal of S-peptide, both fragments retain the ability to bind S-peptide and S-peptide-tagged proteins. The 122cys residue in the mutant fragment is available for site-specific conjugation.

journal_name

Protein Expr Purif

authors

Backer MV,Gaynutdinov TI,Aloise R,Przekop K,Backer JM

doi

10.1016/s1046-5928(02)00546-6

keywords:

subject

Has Abstract

pub_date

2002-12-01 00:00:00

pages

455-61

issue

3

eissn

1046-5928

issn

1096-0279

pii

S1046592802005466

journal_volume

26

pub_type

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