Chemical Forums

Chemistry Forums for Students => Organic Chemistry Forum => Topic started by: HB on January 23, 2014, 01:30:39 PM

Title: hydrolysis of peptide bond
Post by: HB on January 23, 2014, 01:30:39 PM

I want to hydrolyze ethyl N-stearoylglycinate. I have similar procedure that use NaOH in THF/methanol mixture and work at room temp 5 h.
I am asking if I refluxed the peptide in aq. NaOH for shorter time, does this affect the peptide bond instead of or beside ester hydrolysis

Title: Re: hydrolysis of peptide bond
Post by: AlphaScent on January 23, 2014, 02:31:56 PM

Heat and base can always possibly allow for other side reactions.  Why would you fix what isn't broken if the first conditions give the desired product?

If you want to know, try it.  As Disco would say,

"Organic chemistry is an experimental science"

Title: Re: hydrolysis of peptide bond
Post by: orgopete on January 24, 2014, 10:10:37 AM

I think you should be safe as amide bonds must form a dianion to eject a very basic RNH(-). So, provided you do not overwhelm the reaction with excess NaOH and there is sufficient solubility for reaction, I think you should be fine.

Title: Re: hydrolysis of peptide bond
Post by: PhDoc on February 08, 2014, 03:25:30 PM

If there's any way you can do this with a resin-bound enzyme, then do it. The results are sweet.