Search

A peptide consisting of the first 21 residues of human myelin basic protein (MBP) was synthesized. The N-terminal alanine of portions was blocked in separate experiments with alkyl carboxylates varying in size from 2 to 10 carbon atoms. The effects of these different alkyl carboxylates at the N-terminus on the secondary structure was studied by circular dichroism (250-190 nm). In water, the spectra of the unblocked peptide suggested unordered structure with large negative ellipticities at 198 nm. Addition of an acetyl group altered the magnitude of [theta]198 from -21856 +/- 2319 to -11095 +/- 1000 deg cm2 dmol-1, suggesting a significant increase in ordered structure. When peptides with longer alkyl carboxylates, acylated at the N-termini, were studied, the magnitude of theta 198 approached that of the unblocked peptide but greater negative ellipticities were observed for the C8 and C10 alkyl carboxylates. The theta 222 values were generally low (-1803 +/- 463) but increased with increasing length of the alkyl carboxylate to about -3200 deg cm2 dmol-1, suggesting that little alpha-helical structure was present. The spectra were also taken in lipid-mimetic solvents, including 2-propanol, methanol, and lysophosphatidylglycerol (lysoPG). In general the theta 198 and theta 222 values were suggestive of increased structure in these environments compared to water. In 90% 2-propanol the theta 198 of the unblocked peptide did not change when an acetyl group was added to the N-terminus (9088 compared to 8477 deg cm2 dmol-1). Addition of longer alkyl carboxylates correlated with larger, negative ellipticities.(ABSTRACT TRUNCATED AT 250 WORDS)