The ability to control the specific conformation of peptides or proteins is highly desirable in the design of bioactive materials,[1] optical data storage devices,[2] or for triggering the folding/unfolding of oligopeptide chains.[3, 4] Conformational changes in macromolecules can be achieved by incorporating a photoresponsive “monomer” into the molecule backbone;[5] such a monomer is capable of converting light energy into a permanent change in geometry. This approach is also seen in biological receptors[6–9] where the photoisomerization of organic chromophores is used to switch between different conformations. One of the most prominent examples of such switches is the protonated Schiff base (PSB) of retinal found in rhodopsin proteins. This chromophore undergoes a cis!all-trans photoisomerization that triggers a conformational change of the native protein scaffold.
Mechanism of the initial conformational transition of a photomodulable peptide
De Angelis, Filippo;
2005
Abstract
The ability to control the specific conformation of peptides or proteins is highly desirable in the design of bioactive materials,[1] optical data storage devices,[2] or for triggering the folding/unfolding of oligopeptide chains.[3, 4] Conformational changes in macromolecules can be achieved by incorporating a photoresponsive “monomer” into the molecule backbone;[5] such a monomer is capable of converting light energy into a permanent change in geometry. This approach is also seen in biological receptors[6–9] where the photoisomerization of organic chromophores is used to switch between different conformations. One of the most prominent examples of such switches is the protonated Schiff base (PSB) of retinal found in rhodopsin proteins. This chromophore undergoes a cis!all-trans photoisomerization that triggers a conformational change of the native protein scaffold.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
