Influence of collagen denaturation on the nanoscale organization of adsorbed layers

Viscoelastic adlayers of collagen and lysozyme studied using quartz crystal microbalance with dissipation monitoring

“…Despite a common appearance in the f-t and D-t plots, CSC at pH 3 with salt and at pH 7 must be in essentially different states, as indicated by the different D/ f and the CD information. Although the adsorption with a large relaxation has been reported using QCM-D for some fibrous proteins such as collagen [21,26] and fibronectin [27,28], a two-step adsorption, as found in the current study, rarely appears. It may have been overlooked in part because most previous studies were conducted using buffer solutions, and we have shown that two-step adsorption is easily obscured in the presence of salt.…”

Viscoelastic properties of adsorbed and cross-linked polypeptide and protein layers at a solid–liquid interface

“…The principles behind this technique have been reported elsewhere [12]. The measurement of changes in frequency and dissipation using QCM-D allows one to estimate the viscoelasticity of the non-elastic adsorbed layer by using Voigt viscoelastic model [13][14][15], which has been used to probe the rheological properties of proteins [16,17] and synthetic polymers [18][19][20] at the solid-liquid interface. Höök et al [16] used this model to study the viscoelasticity of an adsorbed Mytilus edulis foot protein (Mefp-1) film both before and after cross-linking of the adsorbed layer by NaIO 4 .…”

Understanding and controlling type I collagen adsorption and assembly at interfaces, and application to cell engineering

“…2b. On images obtained under water, some aggregates are terminated by a rootlike structure [18]. This appears even more clearly when imaging is performed on dried samples [21].…”

“…They are not formed upon drying, and can easily be observed under liquid on wet samples, although with a lower resolution [12,13,17,18]. Collagen supramolecular structures with different geometries may also be obtained through dewetting.…”

“…2b) [18]. High resolution AFM images were acquired to elucidate the structure of the interfacial collagen aggregates, as presented in Fig.…”