Abstract
Four derivatives of the bioactive fragment 6–11 of Substance P were characterized by means of one- and two-dimensional 1H n.m.r. spectroscopy. Indirect evidence of backbone folding for these hexapeptides was given by temperature coefficients and paramagnetic relaxation rate enhancements of the amide protons. Chemical modifications were found to modulate the solution structure. Retro-inversion caused some conformational changes and a correlation between these structural variations and the relative biological activities was attempted.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have