The affinity of a synthesized amphiphilic peptide to bind Chi has been studied. It was shown that the peptide, which contains histidine, is able to stabilize the dimeric form of Chi in aqueous solution, making the pigment-peptide complex. The interaction between Chi and the amphiphilic peptide, without support of histidine, caused, the formation of higher pigment aggregates based on the hydrophobic interaction only. The dimer of Chl ligated to the peptide by the histidine residue showed that the absorption at 685 nm could serve as an in vitro model of the Chi a special dimer. The size and molecular weight of the Chi-peptide complex was estimated. (C) 1999 Elsevier Science S.A. All rights reserved.