Abstract
We report a molecular simulation study to investigate a helical peptide (β-adrenoceptor) confined in two metal-organic frameworks (MOFs) namely IRMOF-74-II and -III. Reversible structural transformation between the major (α-helix and 310-helix) and minor structures (bend, turn and coil) of the confined peptide is observed. In IRMOF-74-II, the peptide is over-confined and the helicity is lower compared to that in bulk water; however, the helicity is enhanced upon moderately confined in IRMOF-74-III. As attributed to the loss of conformational entropy, the thermal fluctuations of the peptide in both MOFs are smaller than in bulk water. The hydrophobic solvent-accessible surface area of the peptide, in contrast to the hydrophilic counterpart, is largely reduced upon confined in both MOFs because of the favorable interactions between hydrophobic residues and MOFs. This study provides microscopic insight into β-adrenoceptor peptide confined in MOFs and might be useful toward the rational design of nano-carriers for peptides and other biomolecules.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
