Eudenilson Albuquerque / Jonas Oliveira / Umberto Fulco
Librería Samer Atenea
Librería Aciertas (Toledo)
Kálamo Books
Librería Perelló (Valencia)
Librería Elías (Asturias)
Donde los libros
Librería Kolima (Madrid)
Librería Proteo (Málaga)
In this work, the stability of the homotrimeric peptide T3-785, a representative model of human collagen, was described in energetic terms using the molecular fractionation with conjugated caps (MFCC) technique and within the scope of density functional theory (DFT). It was possible to predict the individual relevance of the amino acids Pro, Hyp, Gly, Ile, Thr, Gly, Ala, Arg, Gly, Leu and Ala, the consequent importance of the triads Pro-Hyp-Gly, Ile-Thr-Gly, Ala-Arg-Gly and Leu-Ala-Gly, and finally the influence of the N-terminal, Central and C-terminal zones of each chain in maintaining the integrity of the collagen triple helix. To make this possible, the forces of attraction and repulsion of the 90 residues that make up the system were calculated. Each of these residues had an interaction energy that varied depending on the chemical nature of its side chain, the microsolvation environment surrounding it and the intermolecular contacts it established. The pioneering study of the conformational stability in energetic terms of a free region of imino acids will encourage research focused on the development and synthesis of high-stability artificial collagens by Bioengineering.
