Crystal structure of a dipeptide Boc-Aib-Phe-OMe

R. Balakrishnan, R. Parthasarathy, N. Ramasubbu

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


In order to understand the effect of the restrictions posed by the Aib residue on peptide conformation we studied the crystal structure of a dipeptide t Boc-Aib-Phe-OMe. Crystals of this compound are triclinic, space group P1 with α = 9.600(1)Å, b = 10.262(1) Å, c = 10.799(1) Å, α = 98.43°(1), β = 99.18(1), γ = 98.87°(1). V = 1021.69(18) Å3 and Z=2. The structure was solved by direct methods and refined to an R-Factor of 4.98%. The backbone conformational angles for the Aib residue in molecule A are in the left-handed helical region, while in molecule B they are in the right- handed helical region. The Phe residue in molecule A is in the right-handed helical conformation, while in molecule B it is in the β-region. The peptide units are trans and show significant deviation from planarity [ω1 = 166.67(5) and ω2 = -177.9(5)].

Original languageEnglish (US)
Pages (from-to)371-374
Number of pages4
JournalJournal of Peptide Research
Issue number5
StatePublished - 1997
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Endocrinology


  • Aib
  • Conformation
  • Dipeptide
  • α-helix


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