Version 1
: Received: 18 April 2024 / Approved: 18 April 2024 / Online: 18 April 2024 (14:10:36 CEST)
How to cite:
Lisowska, A.; Swiatek, P.; Debicki, F.; Lewinska, A.; Marciniak, A.; Pacini, L.; Papini, A.M.; Brasun, J. The Role of the Unbinding Cycle on the Coordination Abilities of the Bi-Cyclopeptides Toward Cu(II) Ions. Preprints2024, 2024041255. https://doi.org/10.20944/preprints202404.1255.v1
Lisowska, A.; Swiatek, P.; Debicki, F.; Lewinska, A.; Marciniak, A.; Pacini, L.; Papini, A.M.; Brasun, J. The Role of the Unbinding Cycle on the Coordination Abilities of the Bi-Cyclopeptides Toward Cu(II) Ions. Preprints 2024, 2024041255. https://doi.org/10.20944/preprints202404.1255.v1
Lisowska, A.; Swiatek, P.; Debicki, F.; Lewinska, A.; Marciniak, A.; Pacini, L.; Papini, A.M.; Brasun, J. The Role of the Unbinding Cycle on the Coordination Abilities of the Bi-Cyclopeptides Toward Cu(II) Ions. Preprints2024, 2024041255. https://doi.org/10.20944/preprints202404.1255.v1
APA Style
Lisowska, A., Swiatek, P., Debicki, F., Lewinska, A., Marciniak, A., Pacini, L., Papini, A.M., & Brasun, J. (2024). The Role of the Unbinding Cycle on the Coordination Abilities of the Bi-Cyclopeptides Toward Cu(II) Ions. Preprints. https://doi.org/10.20944/preprints202404.1255.v1
Chicago/Turabian Style
Lisowska, A., Anna Maria Papini and Justyna Brasun. 2024 "The Role of the Unbinding Cycle on the Coordination Abilities of the Bi-Cyclopeptides Toward Cu(II) Ions" Preprints. https://doi.org/10.20944/preprints202404.1255.v1
Abstract
Bicyclic peptides have attracted the interest of pharmaceutical companies because of their remarkable properties putting them on a new path in medicine. Their conformational rigidity that improves proteolytic stability, leads to rapid penetration into tissues via any possible route of administration and elimination, occurring by renal metabolism, is of great importance for people with a history of liver diseases. In addition, each ring can function independently, making them extremely versatile molecules for further optimization. In this paper we compared the potentiometric and spectroscopic properties studied by UV-Vis, MCD, and EPR, of four synthetic analogues of the bi-cyclic peptide c(PKKHP-c(CFWKTC)-PKKH). In particular we correlated the structural and spectral properties of complexes with coordinating abilities toward Cu(II) ions of MCL (Ac-PKKHPc(CFWKTC)PKKH-NH2) that contains the unbinding cycle and N- and C-terminal linear parts, with two histidine residues, one per part; two monocyclic ligands containing one histidine residue, both in the N-terminal position i.e., MCL2 (Ac-PKKHPc(CFWKTC)PKKS-NH2) and in the C-terminal position i.e., MCL3 (Ac-PKKSPc(CFWKTC)PKKH-NH2), respectively, and the linear structure LNL (Ac-PKKHPSFWKTSPKKH-NH2).
Keywords
bi-cyclopeptide; histidine; metal complex; copper ions; stability constant; spectroscopic studies
Subject
Chemistry and Materials Science, Other
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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