| Abstract: | The immunogenicity of a folded, all D -amino acid protein- rubredoxin, has been compared with that for the corresponding L -protein enantiomer. Following multiple administrations with alum adjuvant, the L -protein induced a strong, specific lgG antibody response, whereas the D -protein did not. This relative lack of responsiveness to the D -protein cannot be attributed to rapid excretion, since it is retained at least 4 times longer than the natural L -protein. These observations provide the first direct evidence that a folded D -amino acid protein has low immunogenicity and is long lived in vivo. Proteins with such properties may be useful as molecular platforms in a variety of chemical and pharmaco-logical applications. © 1993 Wiley-Liss, Inc. |
