'Genetic Code'' is Completed with the ''Proteomic Code'' and ''Nucleic Acid Assistged Proterin Folding''

June 12, 2012 (MMD Newswire) -- A major development started in molecular biology and biotechnology industry with discovering of "Proteomic Code(1)" and "Nucleic Acid Chaperons(2)". A US Patent has recently been granted for biotechnological application of the "Proteomic Code" for design and "to Obtain Oligo-peptides Oligo-peptides with High Affinity to Query Proteins".

PRESS CONFERENCE: Boston Convention & Exhibition Center, MA - Monday, June 18th 2012, 10.00 AM EDT, - Boston Convention & Exhibition Center, MA.

The Genetic Code (Nirenberg, 1964) describes the rules how genetic information in nucleic acids is translated into proteins, the "executors" of biological functions. However this code is "degenerate", 61 codons codes 20 amino acids, i.e. 2/3 rd of genetic information is "lost" during translation. On the other hand the native, coded proteins, - as they leave the translation - are often not functional, because their 3D structure remains to be defined. Consequently there is an excess of information in nucleic acids and a shortage of information in the corresponding, translated proteins.

This intriguing equation is now solved. The canonical Genetic Code contains a second code, called the Proteomic Code. This code provides instructions for the coded proteins regarding 3D folding and specific, high affinity interactions with other proteins.

The concept of Proteomic Code emerged already in 1981. However the massive supply of genetic data (for example the Human Genome Project) and the development of bioinformatics and computers were necessary to the correct formulation of the "Proteomic Code" and introducing the revolutionary concept of "Nucleic Acid Assisted Protein Folding (mRNA chaperons)".

Completing the Genetic Code and understanding (utilizing) its redundancy is of course a major scientific discovery. But more than that, it opens the way to rational, de novo design of interacting proteins. Proteins, which are able to specifically and with high affinity interact with each other (affinity peptides, like receptors to ligands or antibodies to antigens) are usually obtained in vivo (immunization of an animal). Computer design of molecular interactions is painstakingly laborious (like docking) and notoriously unreliable. Therefore the "Proteomic Code" is a very welcomed development for the biotechnology industry because it simplifies, rationalizes and radically improves the efficiency of affinity protein design. A US patent is granted recently for

"System and Method to Obtain Oligo-peptides with High Affinity to Query Proteins" (Patent No.: US 8,145,437, B2; Date of Patent: Mar. 27, 2012; patent term extension 1176 days, www.google.com/patents/US8145437.pdf).

This new class of rationally designed affinity peptides is called AFFISEQ® and a company has been founded to introduce the concept and products to the biotechnology and academic community. The company is positive to collaboration, partnering or direct technology transfer. We are available for personal discussion on the Bio2012 in Boston, June 18-21, 2012.

(1) Biro, JC: The Proteomic Code: a molecular recognition code for proteins. Review. Theoretical Biology and Medical Modelling2007, 4:45, http://www.tbiomed.com/content/4/1/45

(2) Biro JC: Nucleic acid chaperons: a theory of an RNA-assisted protein folding. Theor Biol Med Model 2005, 2:35. http://www.tbiomed.com/content/2/1/35

Contact person: Jan C Biro - [email protected] , +1 213 627 6134

Prof. Jan C Biro MD., PhD - CEO
Affiseq® Corp & Homulus Fnd.
Los Angeles, CA, USA
[email protected]
1 213 627 6134