2026-09-20T14:17:42Zhttps://dspace.mit.edu/server/oai/requestoai:dspace.mit.edu:1721.1/366852022-01-13T07:54:36Zcom_1721.1_7582com_1721.1_7581col_1721.1_131024
Richard T. Lee.
Was, Adam (Adam S.)
Massachusetts Institute of Technology. Dept. of Mechanical Engineering.
Massachusetts Institute of Technology. Department of Mechanical Engineering
2007-03-12T17:44:16Z
2007-03-12T17:44:16Z
2006
2006
http://hdl.handle.net/1721.1/36685
77536995
Thesis (S.B.)--Massachusetts Institute of Technology, Dept. of Mechanical Engineering, 2006.
Includes bibliographical references (p. 87-89).
Four novel recombinant protein constructs were designed to improve the delivery of insulin-like growth factor-1 (IGF-1). The IGF-1 sequence was subcloned into a HisMax plasmid and expressed at low levels by transient transfection in 293 cells. Site-specific mutagenesis was used to insert all four construct sequences into the IGF-1 HisMax plasmid, and to insert a secretory sequence into all four construct plasmids. A stable cell line selection in 293 and CHO cells using Zeocin was attempted. The four construct sequences were then subcloned from the HisMax plasmids to TrcHis plasmids and expressed in bacteria for higher production efficiency. Ni-NTA purified protein was detected in three of the four constructs. These proteins may ultimately be useful for myocardial delivery of IGF-1 to facilitate cardiac repair.
by Adam Was.
S.B.
89 p.
eng
Massachusetts Institute of Technology
M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.
http://dspace.mit.edu/handle/1721.1/7582
Mechanical Engineering.
Novel recombinant protein constructs for improved insulin-like growth factor-1 delivery
Novel recombinant protein constructs for improved IGF-1 delivery
Thesis
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<Abstract>Four novel recombinant protein constructs were designed to improve the delivery of insulin-like growth factor-1 (IGF-1). The IGF-1 sequence was subcloned into a HisMax plasmid and expressed at low levels by transient transfection in 293 cells. Site-specific mutagenesis was used to insert all four construct sequences into the IGF-1 HisMax plasmid, and to insert a secretory sequence into all four construct plasmids. A stable cell line selection in 293 and CHO cells using Zeocin was attempted. The four construct sequences were then subcloned from the HisMax plasmids to TrcHis plasmids and expressed in bacteria for higher production efficiency. Ni-NTA purified protein was detected in three of the four constructs. These proteins may ultimately be useful for myocardial delivery of IGF-1 to facilitate cardiac repair.</Abstract>
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