Refine
Year of publication
- 2012 (1277) (remove)
Document Type
- Article (1277) (remove)
Keywords
- Curriculum Framework (17)
- European values education (17)
- Europäische Werteerziehung (17)
- Familie (17)
- Family (17)
- Lehrevaluation (17)
- Nachhaltigkeit (17)
- Politik (17)
- Studierendenaustausch (17)
- Unterrichtseinheiten (17)
Institute
- Institut für Physik und Astronomie (175)
- Institut für Biochemie und Biologie (174)
- Institut für Geowissenschaften (142)
- Institut für Chemie (140)
- Institut für Romanistik (65)
- Department Psychologie (60)
- Department Linguistik (47)
- Institut für Ernährungswissenschaft (38)
- Wirtschaftswissenschaften (32)
- Historisches Institut (31)
The c-Fosc-Jun complex forms the activator protein 1 transcription factor, a therapeutic target in the treatment of cancer. Various synthetic peptides have been designed to try to selectively disrupt the interaction between c-Fos and c-Jun at its leucine zipper domain. To evaluate the binding affinity between these synthetic peptides and c-Fos, polarizable and nonpolarizable molecular dynamics (MD) simulations were conducted, and the resulting conformations were analyzed using the molecular mechanics generalized Born surface area (MM/GBSA) method to compute free energies of binding. In contrast to empirical and semiempirical approaches, the estimation of free energies of binding using a combination of MD simulations and the MM/GBSA approach takes into account dynamical properties such as conformational changes, as well as solvation effects and hydrophobic and hydrophilic interactions. The predicted binding affinities of the series of c-Jun-based peptides targeting the c-Fos peptide show good correlation with experimental melting temperatures. This provides the basis for the rational design of peptides based on internal, van der Waals, and electrostatic interactions.