Native collagen fibrils from echinoderms are molecularly bipolar.

Collagen fibrils are generally assumed to be cylinders with uniform diameters (except possibly at their ends) and to be composed of molecules all of which have the same polarity. These assumptions have been largely untested because of the extreme difficulty associated with isolating entire native fibrils. Intact collagen fibrils are readily extracted from certain echinoderms, however, and we have therefore analyzed the molecular structure of these fibrils. Our electron microscopic analyses show the above assumptions to be false: echinoderm fibrils, which previously have been shown to be symmetrically spindle shaped, are also molecularly bipolar. Their constituent molecules have their N-termini oriented toward the nearest fibril end, and they are antiparallel in the fibril center. The shape and molecular arrangement of these fibrils have implications for fibrillogenesis.