Towards the design of host–guest complexes: biotin and urea derivatives versus artificial receptors

• Published in: Biosensors & bioelectronics Vol. 20; no. 6; pp. 1242 - 1249
• Main Authors: Claramunt, Rosa M., Herranz, Fernando, María, M. Dolores Santa, Jaime, Carlos, Federico, Miguel de, Elguero, José
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Lausanne Elsevier B.V 15.12.2004; Elsevier Science
• Subjects: Barbital; Binding Sites; Biological and medical sciences; Biomimetics - methods; Biotechnology; Biotin; Biotin - analogs & derivatives; Biotin - analysis; Computer Simulation; Drug Design; Fundamental and applied biological sciences. Psychology; Methods. Procedures. Technologies; Models, Chemical; Models, Molecular; Molecular modeling; NMR spectroscopy; Others; Protein Binding; Receptors; Receptors, Cell Surface - chemistry; Urea; Urea - analogs & derivatives; Urea - analysis; Various methods and equipments; Urea; Receptors; Biotin; NMR spectroscopy; Barbital; Molecular modeling; Receiver; NMR spectrometry; Complexes; Modeling; Comparative study
• ISSN: 0956-5663; 1873-4235
• DOI: 10.1016/j.bios.2004.05.019

Molecular mechanics calculations (Macromodel v.5.0 and v.8.1) have been used in order to correlate the minimized energies of the complexes with the binding constant K b values measured on two hosts and five urea derivatives including methyl biotin. K b values obtained by means of NMR titrations, in the right concentration range between 20 and 80% of saturation, correlate well with the energies provided by the molecular modeling study of the complexes.