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The extracellular matrix of the dermis is a complex, dynamic system with the various dermal components undergoing individual physiologic changes as we age. Age-related changes in the physical properties of collagen were investigated in particular by measuring the effect of aging, most likely due to the accumulation of advanced glycation end product (AGE) cross-links, on the nanomechanical properties of the collagen fibril using atomic force microscope nano-indentation. An age-related decrease in the Young's modulus of the transverse fibril was observed (from 8.11 to 4.19 GPa in young to old volunteers, respectively, P<0.001). It is proposed that this is due to a change in the fibril density caused by age-related differences in water retention within the fibrils. The new collagen-water interaction mechanism was verified by electronic structure calculations, showing it to be energetically feasible.

Pertenece a

UCL University College London Eprints  


Ahmed, T -  Nash, A -  Clark, KE -  Ghibaudo, M -  de Leeuw, NH -  Potter, A -  Stratton, R -  Birch, HL -  Enea Casse, R -  Bozec, L - 

Id.: 69836812

Idioma: eng  - 

Versión: 1.0

Estado: Final

Tipo:  text - 

Palabras claveadvanced glycation end products, aging, atomic force microscopy, collagen, nanomechanics, nanotechnology - 

Tipo de recurso: Article  - 

Tipo de Interactividad: Expositivo

Nivel de Interactividad: muy bajo

Audiencia: Estudiante  -  Profesor  -  Autor  - 

Estructura: Atomic

Coste: no

Copyright: sí

: open

Formatos:  text - 

Requerimientos técnicos:  Browser: Any - 

Relación: [IsBasedOn] International Journal of Nanomedicine , 12 pp. 3303-3314. (2017)

Fecha de contribución: 20-may-2017



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