Catalytic effects of histidine enantiomers and glycine on the formation of dileucine and dimethionine in the salt-induced peptide formation reaction.
The salt-induced peptide formation (SIPF) reaction takes place readily under mild reaction conditions and proceeds via a copper complex. Its ease of reaction and the universality for prebiotic scenarios add weights to the arguments in favour of the importance of peptide and proteins in the tug of war with the RNA world hypothesis. In addition, the SIPF reaction has a preference for L-form amino acids in dipeptide formation, casting light on the puzzle of biohomochirality, especially for the amino acids with aliphatic side chains. A detailed investigation on the behaviour of aliphatic leucine in the SIPF reaction is presented in this paper, including the catalytic effects of glycine, L- and D-histidine as well as the stereoselectivity under all the reaction conditions above. The results show a relatively low reactivity and stereoselectivity of leucine in the SIPF reaction, while both glycine and histidine enantiomers remarkably increase the yields of dileucine by factors up to 40. Moreover, a comparative study of the effectiveness of L- and D-histidine in catalysing the formation of dimethionine was also carried out and extends the scope of mutual catalysis by amino acid enantiomers in the SIPF reaction.
Li
Feng
F
Faculty of Chemistry and Pharmacy, Institute of General, Inorganic and Theoretical Chemistry, University of Innsbruck, Innsbruck, Austria.
Fitz
Daniel
D
Fraser
Donald G
DG
Rode
Bernd M
BM
D002384:Catalysis; D019281:Dimerization; D005998:Glycine / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D007930:Leucine / Q000737:chemistry*; D008715:Methionine / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D012965:Sodium Chloride / Q000737:chemistry*; D013237:Stereoisomerism
D010455:Peptides; D012965:Sodium Chloride; D006639:Histidine; D008715:Methionine; D007930:Leucine; D005998:Glycine