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Research Letter: Retroinverso Mimetics of S Peptide
Author(s) -
Rai Jagdish
Publication year - 2007
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/j.1747-0285.2007.00595.x
Subject(s) - peptide , rnase p , circular dichroism , ribonuclease , chemistry , peptide sequence , protein structure , peptide conformation , stereochemistry , biochemistry , rna , gene
The S peptide from ribonuclease S was used as a model system to explore the relationship between the native peptide and its retroinverso (RI) analog. As probed by circular dichroism, the conformations of S peptide and retroinverso S peptide (RIS peptide) are each right‐handed helical conformation. The helical propensity of retro S peptide is greater than S peptide, in trifluoroethanol (TFE). In 70% TFE, the S peptide possesses greater helicity at pH 4 than at pH 7, whereas RIS peptide possesses greater helicity at pH 7 than at pH 4. The RIS peptide does not mimic the S peptide in binding to S protein. Specifically, the RIS peptide does not mimic the S peptide to effect RNase activity with S protein and it also does not inhibit the RNase activity of S peptide with S protein. The biological mimicry between the S peptide and its RIS analog depends on the conformation and relatedness of both the side chain and backbone substructures. The backbones in the S peptide and its RIS analog are reverted with respect to each other; however, the side chain patterns are predicted to be similar. Importantly, if the molecular interactions of backbone atoms of the S peptide and its binding to S protein, then the RIS analog would be unlikely to mimic this parent peptide.