Celebrating one year of the peptide synthesis and purification blog!

Wow! I can’t believe it’s been a year since this whole blogging adventure started.  This started as a technical resource for me and my colleagues within the peptide synthesis and purification space.  The idea was to enable easy access to some of the hard-to-find answers for common questions that I have encountered working with different peptide groups.

The blog has grown steadily this year and for that I thank you.  In the following post, I’ll highlight a few of the most popular posts from the past year as well a few of my favorites.  I hope you will consider providing feedback using the survey link so that we can continue to grow, keeping the content interesting and relevant.

Over the past year, we have published almost 30 blogs with topics that focus on both synthesis techniques and tricks as well as purification of peptide using flash chromatography, admittedly a new space for me.

The most popular post to date evaluates the lifetime of amino acids in solution.  Some weird things happened when I left amino acids sealed, but not nitrogen sparged at room temperature for more than a month, but when stored in the fridge, the synthesis turned out great!  Nice to know that amino acid solutions have a lifetime, as I’m sure you all agree that weighing out and dissolving amino acids is the worst part of setting up a synthesizer.

Next in popularity is a purification topic highlighting the difference in retention, and sometimes even purification efficiency that can be observed by choosing a different stationary phase.  This is particularly important if you’re trying to purify a particularly hydrophobic peptide.  Choosing a less retentive stationary phase can help you save time and solvent in these challenging purifications.

Second runner up in the popularity contest is the first of two discussions about resin choice for peptide synthesis.  What loading level can you really get away with?  While it seems somewhat trivial, the resin choice can really set your synthesis up for success or potentially failure as I was able to demonstrate.

Writing this blog has given me the opportunity to really experiment and dabble in some method development in the peptide synthesis and purification space.  One of my favorite experiments recently was when I stacked two cartridges with differing stationary phases in line for a single purification.  The purification turned out excellent (>95% purity), but the most interesting part was how the separation profile changed depending on the orientation of the two cartridges.  Stay tuned for more work in this area with a more diverse panel of peptides.

Another favorite was when I evaluated the stability of Pd for use in allyl/alloc deprotections at room temperature.  Turns out, the Pd was much more stable that I originally expected and I achieved full deprotection.

You all have made this blog a success and I hope it continues to grow.  Look forward to topics next year including: how to use an analytical scouting column to design an effective gradient for purification using flash chromatography and evaluating different conditions to improve the efficiency of depsipeptide unit incorporation.

I’d love to hear from you!  Please don’t hesitate to send along ideas for future posts and don’t forget the to complete the survey if you have a few minutes.

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