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Preferential hydrophobic interactions are responsible for a preference of D-amino acids in the aminoacylation of 5'-AMP with hydrophobic amino acidsWe have studied the chemistry of aminoacyl AMP to model reactions at the 3' terminus of aminoacyl tRNA for the purpose of understanding the origin of protein synthesis. The present studies relate to the D, L preference in the esterification of 5'-AMP. All N-acetyl amino acids we studied showed faster reaction of the D-isomer, with a generally decreasing preference for D-isomer as the hydrophobicity of the amino acid decreased. The beta-branched amino acids, Ile and Val, showed an extreme preference for D-isomer. Ac-Leu, the gamma-branched amino acid, showed a slightly low D/L ratio relative to its hydrophobicity. The molecular basis for these preferences for D-isomer is understandable in the light of our previous studies and seems to be due to preferential hydrophobic interaction of the D-isomer with adenine. The preference for hydrophobic D-amino acids can be decreased by addition of an organic solvent to the reaction medium. Conversely, peptidylation with Ac-PhePhe shows a preference for the LL isomer over the DD isomer.
Document ID
Document Type
Reprint (Version printed in journal)
External Source(s)
Lacey, J. C. Jr
(University of Alabama Birmingham)
Wickramasinghe, N. S.
Sabatini, R. S.
Date Acquired
August 22, 2013
Publication Date
April 15, 1992
Publication Information
Publication: Experientia
Volume: 48
Issue: 4
ISSN: 0014-4754
Subject Category
Distribution Limits
Non-NASA Center
NASA Discipline Exobiology
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