YMC has launched an application note entitled 'Separation of structurally similar peptides at pH >=7'.
Reverse-phase chromatography is the most powerful method for peptide purification.
In order to improve the cost-effectiveness of industrial-scale peptide purifications, YMC has developed a new hybrid silica base and a novel bonding technology to improve process efficiencies and increase column lifetime.
The hybrid silica base, named YMC-Triart, was successfully prepared using micro-reaction flow technology.
This allows the production of completely spherical, porous beads with a layered hybrid structure.
Compared with conventional silica-based materials, the new hybrid particles show an enhanced stability in alkaline pH mobile phases, allowing a wider flexibility in separation conditions over an extended pH range.
In addition, the hybrid silica gels can be cleaned in place with NaOH-containing buffers.
This improves packed column lifetime in peptide purification processes.
Human angiotensin II and III contain the same seven amino-acid sequences.
Angiotensin II differs from angiotensin III only by an additional N-terminal aspartate.
Structurally similar peptides such as angiotensin II and III can be difficult to separate under the low pH conditions that are typically used for peptide separations.
With the increased pH stability of YMC-Triart, resolution can be increased by using neutral to alkaline pH conditions.
