alne at IBCH.SIOBC.RAS.RU
Wed Feb 21 10:04:02 EST 1996
We would like to collaborate with you and submit a joint research
proposal to U.S. Civilian Research and Development Foundation
We look forward to beginning the dialogue and then to expanding our research
and business relations. If you are interested in cooperation in these mutual
investigation we will greatly appreciate you kindly reply by FAX or E-mail.
Please do not reply to the newsgroup because we are not subscribed.
Dr. A. Wulfson, Ph.D.
Head of the Recombinant Proteins Group
FAX: +7 (095) 330-7274
E-mail: wan at ibch.siobc.ras.ru
General: our research group of biotechnology of recombinant proteins deals
with isolation, purification and production of biologically active human
recombinant proteins such as cytokines and insulin. Recently we carried out
the development of a technological scheme for the production of human
TNF-alpha (wild-type as well as mutants), Il-3 and IFN-gamma. Based upon
strains designed at our Institute, we are developing at present the
technological operation for production of insulin. Results of our
investigation of TNF-alpha will be published in
Russian Journal of Bioorganic Chemistry N3, 1996
(English edition is available)
"An Effective Method of Purification For Human Recombinant Tumor Necrosis
R.V. Tikhonov, S.A. Yakimov, V.G. Korobko, A.N. Wulfson
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry,
Russian Academy of Sciences, 117871, Miklukho-Maklaya St. 16/10,
During the progress of our research work we have faced some problems
connected with preservation of biological activity of rhIFN-gamma.
That's only one reason why we have no opportunity to start the clinical
trials of our product and make promotion of the medicines based on rhIFN-gamma
for clinical applications. To solve this problem we are going to make
experimental work to design more stable variants of rhIFN-gamma in the
following lines of investigation:
1. COMPUTER DESIGN OF PROTEINS
The computer modeling by the molecular dynamics method of protein spatial
structure to determine potential mutation regions which allow formation of
rhIFN-gamma dimer binding by S-S bonds.
2. GENETIC ENGINEERING
a) Preparation of N-terminal deletion mutants lacking 7-10 residues. We
suppose that such shortening will increase the stability of protein and
facilitate its renaturation without lost of protein activity
b). Preparation of mutant analogs of rhIFN-gamma in which the spatial
structure would be stabilized by intermolecular S-S bonds.
3. STRUCTURAL ANALYSIS
Analysis of the protein dimer spatial structure by X-ray analysis or
Isolation and purification of the recombinant protein, its renaturation and
determination of reagents and buffer solutions in which the protein remains
stable during long time periods and can be lyophilized with minimal lost of
We hope that a combination of these approaches would give us the possibility
to design stable substance of protein rhIFN-gamma for our further work.
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