| Autor: |
Larocca M; Istituto di Metodologie per l'Analisi Ambientale-Consiglio Nazionale delle Ricerche (CNR-IMAA), Contrada, Santa. Loja, 85050 Potenza, Italy., Floresta G; Department of Drug and Health Sciences, University of Catania, Viale A. Doria 6, 95125 Catania, Italy., Verderese D; Dipartimento di Scienze Economiche e Statistiche, Università di Salerno, via Giovanni Paolo II, 132, 84084 Salerno, Italy., Cilibrizzi A; Institute of Pharmaceutical Science, King's College London, Stamford Street, London SE1 9NH, UK.; Centre for Therapeutic Innovation, University of Bath, Bath BA2 7AY, UK. |
| Abstrakt: |
The hydrophobic effect is the main factor that drives the folding of polypeptide chains. In this study, we have examined the influence of the hydrophobic effect in the context of the main mechanical forces approach, mainly in relation to the establishment of specific interplays, such as hydrophobic and CH-π cloud interactions. By adopting three oligopeptides as model systems to assess folding features, we demonstrate herein that these finely tuned interactions dominate over electrostatic interactions, including H-bonds and electrostatic attractions/repulsions. The folding mechanism analysed here demonstrates cooperation at the single-residue level, for which we propose the terminology of "single residues cooperative folding". Overall, hydrophobic and CH-π cloud interactions produce the main output of the hydrophobic effect and govern the folding mechanism, as demonstrated in this study with small polypeptide chains, which in turn represent the main secondary structures in proteins. |
