Abstract
Collagen-based biomaterials are expected to become a useful matrix
substance for various biomedical applications in the future. By taking
advantage of the crystallographic data of the triple-helical peptide
T3-785, a collagen-like peptide whose homotrimeric structure presents
large conformational similarity to the human type III collagen, we
present a quantum biochemistry study to unveil its detailed binding
energy features, taking into account the inter-chain interaction
energies of 90 amino acid residues distributed into three interlaced
monomers. Our theoretical model is based on the density functional
theory (DFT) formalism within the molecular fragmentation with conjugate
caps (MFCC) approach. We predict the individual relevance
(energetically) of the amino acid triplets Pro-Hyp-Gly, Ile-Thr-Gly,
Ala-Arg-Gly and Leu-Gly-Ala, as well as the influence of the N-terminal,
central and C-terminal regions, looking for the integrity of the
collagen's triple helix. We found that the amino acid residues
comprising the peptide T3-785 have an interaction energy that depends
not only on the chemical nature of the side chain, but also the
surrounding solvent molecules and inter-chain intermolecular
interactions. The energy profile of this collagen-model molecule depicts
a character essentially attractive to its conformational stability,
encouraging research focusing on the development and synthesis of
artificial collagen with high stability for bioengineering applications.
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