Go natural and smarter: fenugreek as a hydration designer of collagen based biomaterials

被引:12
作者
Kanungo, Ivy [1 ]
Fathima, Nishter Nishad [1 ]
Rao, Jonnalagadda Raghava [1 ]
Nair, Balachandran Unni [1 ]
机构
[1] CSIR, Cent Leather Res Inst, Chem Lab, Madras 600020, Tamil Nadu, India
关键词
DIELECTRIC-PROPERTIES; TISSUE; COMPOSITES; DYNAMICS; RELEASE; WATER; GUM; POLYSACCHARIDES; DIFFERENTIATION; TEMPERATURE;
D O I
10.1039/c4cp04363d
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Collagen-based biomaterials have received considerable attention for smarter biomedical applications due to their inherent superior mechano-biological properties. However, accumulating evidence suggests that water, as a probe liquid bound in collagen, might be investigated to explore the influence of additives on the static and dynamic solvation behavior of collagen. The structure and dynamics of water near the surface/interface of collagen-fenugreek composites were demonstrated via circular dichroic spectroscopy, thermoporometry and impedimetric measurements to enlighten about the configuration-function relationship of collagen. Thermodynamic parameters of the composites signify the fenugreek concentration dependent structural robustness of collagen. Thermodynamic parameters such as free energies for unfolding, enthalpies, entropies and activation energies indicate that the residual structure modulates the stability of the denatured state up to 22 kcal mol(-1) and the parameters correlate with structural data for collagen complexed with fenugreek. The association constant of fenugreek is found to be 0.5807 M-1. The binding of fenugreek influences rearrangement of the collagen-water network, resulting in the transition from a disordered (high entropy) unbound state to a structured (lower entropy) bound state. Fenugreek concentration plays a crucial role in shaping up the free energy that governs the folding, structure and stability of collagen. Dielectric data emphasize the effect of hydrophobic and hydrophilic clusters on the side chain motion constraints. The thermoporometry technique probes the pore size distributions of the composites. These methods provide insights into the role of excluded volume, chain stiffness and stability of a new collagen-galactomannan based composite, expanding its utility in "smart biomaterial applications''.
引用
收藏
页码:2778 / 2793
页数:16
相关论文
共 46 条
  • [1] Effect of sucrose on the thermodynamic properties of ovalbumin and sodium caseinate in bulk solution and at air-water interface
    Antipova, AS
    Semenova, MG
    Belyakova, LE
    [J]. COLLOIDS AND SURFACES B-BIOINTERFACES, 1999, 12 (3-6) : 261 - 270
  • [2] Barnes F.S., 2006, Handbook of Biological Effects of Electromagnetic Fields
  • [3] Dielectric Relaxation Spectroscopy of Lysozyme Aqueous Solutions: Analysis of the δ-Dispersion and the Contribution of the Hydration Water
    Cametti, C.
    Marchetti, S.
    Gambi, C. M. C.
    Onori, G.
    [J]. JOURNAL OF PHYSICAL CHEMISTRY B, 2011, 115 (21) : 7144 - 7153
  • [4] CHANDRAKASAN G, 1976, J BIOL CHEM, V251, P6062
  • [5] Bulk-solvent and hydration-shell fluctuations, similar to α- and β-fluctuations in glasses, control protein motions and functions
    Fenimore, PW
    Frauenfelder, H
    McMahon, BH
    Young, RD
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (40) : 14408 - 14413
  • [6] Collagen for bone tissue regeneration
    Ferreira, Ana Marina
    Gentile, Piergiorgio
    Chiono, Valeria
    Ciardelli, Gianluca
    [J]. ACTA BIOMATERIALIA, 2012, 8 (09) : 3191 - 3200
  • [7] Garti N, 1997, FOOD SCI TECHNOL-LEB, V30, P305
  • [8] Collagen scaffolds for tissue engineering
    Glowacki, Julie
    Mizuno, Shuichi
    [J]. BIOPOLYMERS, 2008, 89 (05) : 338 - 344
  • [9] The Pursuit of a Scalable Nanofabrication Platform for Use in Material and Life Science Applications
    Gratton, Stephanie E. A.
    Williams, Stuart S.
    Napier, Mary E.
    Pohlhaus, Patrick D.
    Zhou, Zhilian
    Wiles, Kenton B.
    Maynor, Benjamin W.
    Shen, Clifton
    Olafsen, Tove
    Samulski, Edward T.
    Desimone, Joseph M.
    [J]. ACCOUNTS OF CHEMICAL RESEARCH, 2008, 41 (12) : 1685 - 1695
  • [10] Determination of the folding of proteins as a function of denaturants, osmolytes or ligands using circular dichroism
    Greenfield, Norma J.
    [J]. NATURE PROTOCOLS, 2006, 1 (06) : 2733 - 2741