The repetitive sequence GGLGY was found in lamprin, the most important matr
ix protein of lamprey annular cartilage by Keeley and co-workers. Similar s
equences appear also in other proteins, i.e. elastin, spidroin, spider mino
r ampullate silk proteins, in matrix proteins of the chorion or egg shell m
embrane of insects and others. We synthesized (GGLGY)(n), n = 1, 2, 6, beca
use the sequence is repeated six times in the aggregated protein. The pepti
des were studied both in solution and in the solid state. Because the CD sp
ectra were dominated by aromatic contribution, we synthesized GGLGF and GGL
GA in order to carefully interpret the CD spectra. The conformational analy
sis suggests that all synthetic peptides do adopt the same secondary struct
ure. In solution the peptides present a flexible conformation with a signif
icant amount of PPII structure. In the solid state PPII, beta -pleated-shee
ts and beta -turns possibly co-exist. (C) 2001 Elsevier Science B.V./Intern
ational Society of Matrix Biology. All rights reserved.