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The uv absorption properties in aqueous solution and the CD pro¬ perties in aqueous and in trifluoroethanol solution have been investigated for co-oligopeptides of tryptophan , phenylalanine and glycine of the general structures H-Gly-X-(Gly) -Trp-Gly-OH, X = Trp or Phe , n = 0,1,2. These have been compared with uv and CD properties of model compounds containing one aromatic residue (i.e. H-Trp-Gly-OH , H-Gly-Trp-OH , H-Gly-Trp-Gly-OH and H-Phe-Gly-OH , H-Gly-Phe-OH , H-Gly-Phe-Gly-OH) or two aromatic residues (i.e. H-Trp-Trp-OH , H-Trp-Trp-Gly-OH , H-Gly-Trp-TrpOH and H-Phe-Trp-OH , H-Phe-Trp-Gly-OH , H-Gly-Phe-Trp-OH). The uv absorption spectra have been analyzed in terms of the chromophoric contributions of the two aromatic side chains and of the peptide bond. No interaction leading to a modification of the uv absorption spectra (e.g. stacking , charge-transfer complexation) has been detected between the two aromatic side chains of the investigated co-oligopeptides. The mean absorption contribution of the peptide bond (6910 M cm ) suggests that the backbone of the investigated peptides is mostly in a disordered conformational state and excludes the possibility of a formation of helical structures for the longer peptides. However the presence of the 3-structure for some of the products is not excluded. In the CD spectra there are evidences of a chromophoric interac¬ tion between the two aromatic moieties of the tetrapeptides H-Gly-Trp-Trp-Gly-OH and H-Gly-Phe-Trp-Gly-OH. On this basis,

Size, shape and intermolecular interactions of fibrinogen in solution