Hello everybody, I am wondering if anybody currently knows of a protocol/method to fold peptides that revolved around the use of methanol? Our Lab Director is convinced one exists but my students and I are having a hard time finding such a method.

 

To be more specific we work with SPPS if anyone has any general questions on that as well

Methanol would denature the protein, not assist it in folding. Maybe he's talking about the Folch extraction method? I know that trifluoroethanol can help stabilize protein helices, but only in very small concentrations.

 

~EE

I attended a seminar many moons ago which discussed something similar and exposing novel enzyme activities. However, you could cross-reference the following paper:

 

Abstract

The use of enzymes in nearly anhydrous organic solvents generally results in low initial rates/percentage conversions. The current review focuses on some biocatalyst designs like immobilization on nanomaterials, enzyme precipitated and rinsed with organic solvents (EPROS), crosslinked enzyme crystals (CLEC), crosslinked enzyme aggregates (CLEA), protein coated microcrystals (PCMC) and crosslinked protein coated microcrystals (CLPCMC) which show much better catalytic efficiency in such media as compared to other kinds of biocatalyst preparations. The basic methodology and principle behind these efficient designs are described. The relatively recent results on catalytic promiscuity as seen in low water media have also been covered. It is hoped that this will further encourage wider applications of enzymes in neat organic solvents in organic synthesis.

Keywords: Transesterification reactions, aldol condensation, kinetic resolution, enantioselective reactions, regioselectivity, nanobiocatalysts, enzyme catalysis in low water media, enzyme promiscuity

 

 

http://www.hoajonline.com/orgchem/2053-7670/1/1