Chiral recognition of mesoporous SBA-15 with an incorporated chiral porphyrin

The incorporation of a chiral porphyrin into the mesoporous molecular sieves SBA-15 by reactions of the surface OH group with an amino group of the porphyrin and its chiral recognition were studied. The resultant material was analyzed by a combination of techniques and it was confirmed that the channels of SBA-15 have been filled with chiral porphyrins, leaving the mesopores unaffected. The investigation of chiral recognition of the porphyrin and the composite SBA-15 shows that the incorporated SBA-15 has a clear CD spectral signal of the chiral porphyrin and exhibits different chiral recognition abilities for small amino acids. The D-alanine is more tightly bound to the mesoporous composite SBA-15 than its optical antipode.