GAP Peptide Synthesis

Technology #d-1227

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Guigen Li
Professor, Chemistry and Biochemistry, Texas Tech University, Lubbock, TX. Professor Li is interested in the development of new concepts, new achiral and chiral reagents, new reactions, their asymmetric versions and applications. He is also interested in bioorganic and medicinal chemistry, especially, in the study of new analgesic and anti-inflammatory agents, peptide and peptidomimetic drug design, synthesis and structure-activity-relationship (SAR) studies that are important for treating diseases, such as AIDS, cancer and diabetes.
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Cole Seifert
Graduate Student, Chemistry and Biochemistry, Texas Tech University, Lubbock, TX.
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Cameron Smith
Licensing Associate 806-834-6822
Patent Protection

Provisional Patent Application Filed


Peptides are involved in multiple functions of living systems, including cell signalling, the endocrine system, and allosteric enzyme activation and inhibition, and they are an area of research for pharmaceuticals and cancer therapeutics. They are polymers made up of multiple amino acid monomers linked together through peptide bonds. Each amino acid has a carboxyl-terminus (C-terminus) and an amino-terminus (N-terminus), and the C-terminus of one amino acid links to the N-terminus of another amino acid to create a peptide bond. Currently, peptides are synthesized for pharmaceutical use by solid-phase peptide synthesis (SPPS). In this technique, the C-terminus of an amino acid is bound to a solid resin, and the peptide is synthesized by adding amino acids to the N-terminus, one after another, using the industry preferred Fmoc/tBut strategy. The drawback of this method is that much of the mass yielded from the reaction is the left-over resin and not the desired peptide.

The disclosed technology is a potentially novel method for peptide synthesis. It utilizes group-assisted purification (GAP) chemistry in conjunction with solution-phase peptide synthesis (SolPPS). This means that a solid resin is unnecessary to synthesize the desired peptide, leading to a much higher mass yield. The inventors have created desired peptides with over 50% yields and 99% purity. The method allows for use of the Fmoc/tBut strategy to grow the peptide, the industry preferred strategy, and the peptide is purified through precipitation instead of recrystallization of chromatography. The method is potentially patentable in three aspects: the GAP protecting group, the method to synthesize it, and the entire method of peptide synthesis it allows.

Reference Number: D-1227

Market Applications:

  • Pharmaceutical industry
  • Medical technologies

Features, Benefits & Advantages:

  • High yield/purity peptide synthesis
  • Use in conjunction with Fmoc/tBut strategy
  • Ability to scale up to mass production
  • No recrystallization or chromatography

Intellectual Property:

  • A provisional application was filed on December 14, 2015. 

Development Stage:

  • The technology has been tested and a peptide has successfully been created. The inventors are currently attempting to apply the method to longer, more complex peptides.


  • Guigen Li, Professor, Chemistry and Biochemistry, Texas Tech University, Lubbock, TX
  • Cole Seifert, Graduate Student, Chemistry and Biochemistry, Texas Tech University, Lubbock, TX

Keywords: group-assisted purification, solution-phase peptide synthesis, Fmoc peptide synthesis