1H AND 13C NUCLEAR MAGNETIC RESONANCE SPECTRA OF SOME PEPTIDES WITH FIBRINOGEN‐LIKE REACTIVITY

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Abstract
The 1H and 13C spectra of four peptides, l‐Phe‐Val‐Arg‐pNA, d‐Phe‐Val‐Arg‐pNA, l‐Phe‐Pip‐Arg‐pNA and d‐Phe‐Pip‐Arg‐pNA (pNA = p‐nitroaniline, Pip = pipecolic acid residue), have been examined, and deductions made about their conformation in solution. The d‐Phe peptides, which are cleaved especially rapidly by thrombin in water, have structures (in deuterated DMSO) in which the aromatic ring of the d‐Phe residue is folded back over the Val or Pip residue. This arrangement is not found in the l‐Phe peptides. It is proposed that this feature (in which Phe could be situated near Val and near the Arg‐Gly bond of the Aα chain in the three‐dimensional structure of fibrinogen) may be specially advantageous for binding to the enzyme.