Artículo
How procyanidin C1 sticks to collagen: The role of proline rings
Fecha de publicación:
09/2021
Editorial:
Elsevier Science
Revista:
Biophysical Chemistry
ISSN:
0301-4622
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
Molecular interactions between proteins and polyphenols are responsible for many natural phenomena like colloidal turbidity, astringency, denaturation of enzymes and leather tanning. Although these phenomena are well known, there are open questions about the specific interactions involved in the complexation process. In this work, Molecular Dynamic (MD) simulations and the topology of the electron density analysis were used to study the interactions between the flavonoid procyanidin C1 and a collagen fragment solvated in water. Root mean square deviation; root mean square fluctuation and hydrogen bonds occupancy were examined after 50 ns. The interactions were also analyzed by means of the quantum theory of atoms in molecules. Our results show that the main interactions are hydrogen bonds between –OH groups of the polyphenol and C[dbnd]O groups of the peptide bond. Stacking interactions between proline rings and phenol rings, that is C–H⋯π hydrogen bonds, also stabilize the dynamic structure of the complex.
Palabras clave:
HYDROGEN BONDS
,
POLYPHENOL
,
PROLINE
,
PROTEIN
,
STACKING
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(CCT - NORDESTE)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - NORDESTE
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - NORDESTE
Articulos(IQUIBA-NEA)
Articulos de INSTITUTO DE QUIMICA BASICA Y APLICADA DEL NORDESTE ARGENTINO
Articulos de INSTITUTO DE QUIMICA BASICA Y APLICADA DEL NORDESTE ARGENTINO
Citación
Petelski, Andre Nicolai; Pamies, Silvana Carina; Sosa, Gladis Laura; How procyanidin C1 sticks to collagen: The role of proline rings; Elsevier Science; Biophysical Chemistry; 276; 9-2021; 1-9
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