Guptasarma P
Centre for Cellular and Molecular Biology, Hyderabad, India.
FEBS Lett. 1992 Oct 5;310(3):205-10. doi: 10.1016/0014-5793(92)81333-h.
In linear polypeptides, inversion of amino acid chirality (all-L to all-D) achieves a mirroring of side chain positions and interactions in conformational space. A similar mirroring of side chain positions is independently achieved by a reversal of the direction of the peptide backbone (retro modification). Thus, while an all-D chain could be expected to adopt a perfect 'mirror image' of the three-dimensional structure of its parent all-L protein, the retro-all-L chain could be expected to adopt a topological equivalent of such a mirror image, through the symmetry transformations of side chain interactions. These notions, supported by sequence analyses, modelling studies, and evidence relating to the activity of 'retro-inverso' peptides, are extended towards the proposal, that the backbone reversed chain of a large globular protein might recognize the chiral opposite of the parent protein's substrate(s).
在线性多肽中，氨基酸手性反转（全L型到全D型）可实现构象空间中侧链位置和相互作用的镜像。通过肽主链方向的反转（逆向修饰）可独立实现类似的侧链位置镜像。因此，虽然预计全D链会采用其亲本全L蛋白三维结构的完美“镜像”，但通过侧链相互作用的对称变换，预计逆向全L链会采用这种镜像的拓扑等效结构。这些观点得到了序列分析、建模研究以及与“逆向反转”肽活性相关证据的支持，并进一步提出，大型球状蛋白的主链反转链可能识别亲本蛋白底物的手性对映体。
