Key building block of photoresponsive biomimetic systems
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Data publicació2011-02-10
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Abstract
The conformational, electrical, and optical intrinsic
properties of L-phenylazophenylalanine (L-PAP), a nonproteinogenic
photoresponsive amino acid used to modulate the binding
affinity and activity of peptides and proteins, have been systematically
investigated using quantum mechanical calculations, with
special emphasis being put on the trans-to-cis isomerization of the
azobenzene side group. Analyses of the conformational maps and
the minimum-energy conformations, which were obtained using
density functional theory calculations at the B3LYP/6-311þþG(d,
p) level, indicate that the semiextended β is the most favored
conformation for both the trans and cis isomers in the gas phase.
However, water tends to stabilize the helical backbone arrangement,
but only for the cis isomer since this is a sterically forbidden
conformation for the trans one. On the other hand, time-dependent
density functional theory calculations at the BMK/6-311þG(d,p)
level indicate that the peptide backbone does not induce significant
changes in the optical properties of the chromophore. This feature was evidenced by both the small dependence of the πfπ* and nfπ*
transition wavelengths with the backbone dihedral anglesjandψand the resemblance between the transition wavelengths determined for
L-PAP and free azobenzene. In contrast, the dipole moment has been identified as a key property for this photoresponsive amino acid
because of its large dependence on both the peptide backbone and the isomerization state.
CitacióRevilla-López, G. [et al.]. Key building block of photoresponsive biomimetic systems. "Journal of physical chemistry B", 10 Febrer 2011, vol. 115, núm. 5, p. 1232-1242.
ISSN1520-6106
Versió de l'editorhttp://pubs.acs.org/doi/pdfplus/10.1021/jp108341a
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