The Liberty Advantage Fastest cycle times available Greater purity peptides than conventional synthesis Access peptides impossible to synthesize under conventional conditions Totally automated synthesis of up to 12 peptides

The world’s first and only automated
Microwave Peptide Synthesizer!

Make higher purity peptides faster. Microwave energy drives biochemical reactions to completion up to 10 times faster than by conventional methods, resulting in peptides of greater purity than can be produced under conventional methods. Reactions are not just faster; they are more complete when driven by microwave energy. Liberty's unique utilization of microwave energy gives biochemists and other researchers active in the study of proteins the unprecedented ability to synthesize peptides that were previously inaccessible by conventional synthetic methods. However, the Liberty is more than a research platform. The system is capable of synthesizing up to 12 peptides in a day unattended at scales up to 5 mmol, Liberty's unique combination of speed and productivity. No other technology can equal this kind of productivity.

The system’s superior performance is due to the innovative design of its patented, circular cavity. Liberty utilizes a single-mode cavity that “focuses” a homogenous microwave energy field on the sample, ensuring that the sample always receives the optimum amount of energy to drive the reaction. An integrated fiber optic temperature probe provides true in-situ measurement. Liberty’s temperature monitoring capability controls the power output, ensuring faster reactions, higher yields and improved purity.












The system's superior performance is due to the innovative design of its patented, circular cavity. Liberty utilizes a single-mode cavity that "focuses" a homogenous microwave energy field on the sample, ensuring that the sample always receives the optimum amount of energy to drive the reaction. An integrated fiber optic temperature probe provides true in-situ measurement. Liberty's temperature monitoring capability controls the power output, ensuring faster reactions, higher yields and improved purity.

Flexible

• Wide scale range of 0.025 to 5 mmol
• Use up to 25 amino acid reservoirs
• Programmable cleavage & automated resin addition
• Use either 125- or 250-mL amino acid bottles

Liberty is available as a completely automated system with a scale range of 0.025 to 5 mmol. The system is equipped with 20 amino acid reservoirs and 12 external ports. These external ports can be used for adding extra amino acid solutions, activators, solvents, or any user-defined reagent needed, giving users the cost-effectiveness and flexibility of multiple peptide production at an individually programmed scale.

Reliable & Safe

• Variable size sample loops for all amino acid and activator additions
• Sensor detection of all reagents
• All parts that come into contact with chemicals are composed of chemically-inert materials
• Pressure detection for all chemical transfers
• Waste level detection

Liberty completely controls each reaction step in the process. The patent-pending process uses microwave energy at moderate temperatures to shorten reaction times. Liberty’s temperature control and shortened reaction times translate into a reduction in racemization. Microwave energy drives the reaction steps so quickly that product racemization is virtually eliminated. ^1,2

Easy-to-Use

• Unique resin transfer process allows for a single reaction vessel in a less complicated system
• Compact – fits in a standard fume hood
• Easy-to-use software

Compact enough to fit in a standard fume hood, Liberty conserves valuable fume hood space, maximizing laboratory efficiency. The system's easy-to-use, menu-driven software allows operation directly from a host PC workstation, or over an existing network, giving users the flexibility to develop and import peptide sequences from their desktop workstation and monitor the system's performance from any network location.

¹ Lahm, H.W.; Lergier, W.; Manneberg, M.; Knorr, R. Protein Chem. 1988, 7, 258.
² Chen, S.T.; Chiou, S.H.; Wang, K.T. J. Chin. Chem. Soc. 1991.