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Chimeric ribonuclease as a source of human adapter protein for targeted drug delivery

Title: Chimeric ribonuclease as a source of human adapter protein for targeted drug delivery
Authors: Gaynutdinov, Timur I.; Myshkin, Eugene; Backer, Joseph M.; Backer, Marina V.
Publisher Information: Oxford University Press
Publication Year: 2003
Collection: HighWire Press (Stanford University)
Subject Terms: ORIGINAL ARTICLES
Description: Assembled modular complexes for targeted drug delivery can be based on strong non‐covalent interactions between a cargo module containing an adapter protein and a docking tag fused to a targeting protein. We have recently constructed a completely humanized adapter/docking tag system based on interactions between 15 amino acid (Hu‐tag) and 110 amino acid (HuS) fragments of human ribonuclease I (RNase I). Although recombinant HuS can be expressed and refolded into a functionally active form, the purification procedure is cumbersome and expensive, and more importantly, it yields a significant proportion of improperly folded proteins. Here we describe engineering, high‐yield expression, and purification of a chimeric bovine/human RNase (BH‐RNase) comprising 1–29 N‐terminal amino acids of bovine ribonuclease A and 30–127 amino acids of human RNase I. Unlike RNase I, the chimeric BH‐RNase can be cleaved by either subtilisin or proteinase K between A20 and S21, providing a functionally active HuS. The HuS obtained from chimeric BH‐RNase differs from wild‐type HuS by an N24T substitution; therefore, we have reverted this substitution by mutating N24 to T24 in BH‐RNase. This BH‐RNase mutant can also be cleaved by subtilisin or proteinase K yielding wild‐type HuS. The affinity of HuS obtained from BH‐RNase to Hu‐tag is approximately five times higher than that for recombinant HuS, reflecting a higher percentage of properly folded proteins.
Document Type: text
File Description: text/html
Language: English
Relation: http://peds.oxfordjournals.org/cgi/content/short/16/10/771; http://dx.doi.org/10.1093/protein/gzg097
DOI: 10.1093/protein/gzg097
Availability: http://peds.oxfordjournals.org/cgi/content/short/16/10/771; https://doi.org/10.1093/protein/gzg097
Rights: Copyright (C) 2003, Oxford University Press
Accession Number: edsbas.5EDF7C90
Database: BASE