Role of aliphatic alcohols on the stability of rat-tail tendon (RTT) collagen fiber

Usha, R.; Ramasami, T.

doi:10.1002/(sici)1099-0488(19990701)37:13<1397::aid-polb5>3.0.co;2-5

Cited by 17 publications

(7 citation statements)

References 27 publications

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“…The treatment of stress relaxation data for basic chromium sulfate and formaldehyde-crosslinked RTT and native RTT in aqueous alcoholic media have already been explained briefly. [17,32] Since the matrix structure of collagen exhibits anisotropic properties and high levels of inter-and intramolecular organisation, it is not sufficient to treat relaxation in terms of single element model. It is worthwhile to investigate some useful empirical models to describe the stress relaxation data of collagen fibres.…”

Section: Methodsmentioning

confidence: 99%

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Role of Secondary Structure on the Stress Relaxation Processes in Rat Tail Tendon (RTT) Collagen Fibre

2001

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Section: Methodsmentioning

confidence: 99%

“…The collagen fibres were equilibrated in aqueous-alcoholic media where the alcoholic proportions varied as 1, 7, 10 and 20 mol-%. [32] Hydrogen-Bond-Breaking Reagent Urea used in the experiments was of analytical grade. 1, 3 and 6 m urea solutions were prepared by weighing.…”

Section: Hydrogen Ion Concentrationmentioning

confidence: 99%

Role of Secondary Structure on the Stress Relaxation Processes in Rat Tail Tendon (RTT) Collagen Fibre

2001

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“…21 This is explained elaborately elsewhere. 22,23 It is highly probable that the system may be much more complex than a single relaxation process and perhaps could be a multiphasic system. In order to verify this, the stress relaxation behavior was treated as biphasic in nature.…”

Section: Stress Relaxation Experimentsmentioning

confidence: 99%

Effect of pH on dimensional stability of rat tail tendon collagen fiber

Usha

Ramasami

2000

J. Appl. Polym. Sci.

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The organized molecular structure of collagen is related to its dimensional stability. The dimensional stability of collagen arises from the interplay of various intermolecular forces such as covalent, hydrogen bonding, electrostatic interactions, hydrophobic interactions, London or van der Waals forces, and weak interactions. A structure-function relationship exists in collagen. Electrostatic interactions play an important role in dimensional stabilization. The dimensional stability of rat tail tendon (RTT) collagen fiber is affected by the change in the net fixed charge on the molecule as a function of pH. Thermal and mechanical properties are dependent on molecular and lattice orders. The pH dependence of thermal shrinkage, isometric tension, differential scanning calorimetry, swelling behavior, tensile strength, and percent extension and stress relaxation behavior are studied in 0.02M Tris-maleate buffer at pH 4 -8. The observed experimental results provide compelling evidence that electrostatic interactions play an important role in the dimensional stability of RTT collagen.

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“…9,10 Differential scanning calorimetry (DSC) has been employed to study the denaturation processes in fibrils of collagen. [11][12][13][14] The role of aliphatic alcohols in the stability of collagen fibers using DSC 15 and the effect of crosslinking agents on the thermal and thermomechanical stability of rat-tail tendon collagen fiber have been reported. 16 Nevertheless, the potential toxicity of the crosslinking agent is still controversial.…”

Section: Introductionmentioning

confidence: 99%

Behavior of collagen films in presence of structure modifiers at solid–liquid interface

Usha

Dhathathreyan

Mandal

et al. 2004

J Polym Sci B Polym Phys

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Films of soluble collagen extracted from rat‐tail tendon were studied at the solid–solution interface, and the surface energy of the films was evaluated. The films transferred onto solid substrates using the Langmuir–Blodgett film (LB film) technique were characterized using Fourier transform IR attenuated total reflectance spectroscopy and atomic force microscopy. The properties of the protein in contact with different structure modifiers like basic chromium sulfate (BCS) and formaldehyde (HCHO) were analyzed for the effect of various tanning agents on the protein structure. The thermal properties of the films were studied using differential scanning calorimetry. The results show that the film of collagen treated with BCS exhibits an increase in the peak temperature and enthalpy changes compared to the pure collagen as well as the protein with HCHO. These differences are attributed to the changes in the crosslinks arising from both coordinate–covalent and covalent interactions, respectively. The atomic force micrographs showed an increase in order for the collagen film with BCS compared to the HCHO treated analogue. A similar trend is seen in the surface energy parameters of the protein films on solid surfaces on reacting with BCS and HCHO, suggesting a molecular level ordering process in collagen assemblies. © 2004 Wiley Periodicals, Inc. J Polym Sci Part B: Polym Phys 42: 3859–3865, 2004

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Role of aliphatic alcohols on the stability of rat-tail tendon (RTT) collagen fiber

Cited by 17 publications

References 27 publications

Role of Secondary Structure on the Stress Relaxation Processes in Rat Tail Tendon (RTT) Collagen Fibre

Role of Secondary Structure on the Stress Relaxation Processes in Rat Tail Tendon (RTT) Collagen Fibre

Effect of pH on dimensional stability of rat tail tendon collagen fiber

Behavior of collagen films in presence of structure modifiers at solid–liquid interface

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