Hydrated Collagen: Where Physical Chemistry, Medical Imaging, and Bioengineering Meet

被引:9
作者
Momot, Konstantin I. [1 ]
机构
[1] Queensland Univ Technol QUT, Sch Chem & Phys, Brisbane, Qld 4001, Australia
基金
澳大利亚研究理事会;
关键词
ARTICULAR-CARTILAGE; RELAXATION ANISOTROPY; MAGNETIC-RESONANCE; DIFFUSION-TENSOR; MOLECULAR-DYNAMICS; WATER COMPARTMENTS; MICROSCOPIC MRI; SPIN RELAXATION; T-2; RELAXATION; LIQUID WATER;
D O I
10.1021/acs.jpcb.2c06217
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
It is well-known that collagen is the most abundant protein in the human body; however, what is not often appreciated is its fascinating physical chemistry and molecular physics. In this Perspective, we aim to expose some of the physicochemical phenomena associated with the hydration of collagen and to examine the role collagen's hydration water plays in determining its biological function as well as applications ranging from radiology to bioengineering. The main focus is on the Magic-Angle Effect, a phenomenon observed in Nuclear Magnetic Resonance (NMR) spectroscopy and Magnetic Resonance Imaging (MRI) of anisotropic collagenous tissues such as articular cartilage and tendon. While the effect has been known in NMR and MRI for decades, its exact molecu l a r mechanism remains a topic of debate and continuing research in scientific literature. We survey some of the latest research aiming to develop a comprehensive molecular-level model of the Magic-Angle Effect. We also touch on other fields where understanding of collagen hydration is important, particularly nanomechanics and mechanobiology, biomaterials, and piezoelectric sensors.
引用
收藏
页码:10305 / 10316
页数:12
相关论文
共 101 条
[41]  
Hulmes D. J. S., 2008, P15, DOI 10.1007/978-0-387-73906-9_2
[42]   Reversible changes in the 3D collagen fibril architecture during cyclic loading of healthy and degraded cartilage [J].
Inamdar, Sheetal R. ;
Prevost, Sylvain ;
Terrill, Nicholas J. ;
Knight, Martin M. ;
Gupta, Himadri S. .
ACTA BIOMATERIALIA, 2021, 136 :314-326
[43]   Proteoglycan degradation mimics static compression by altering the natural gradients in fibrillar organisation in cartilage [J].
Inamdar, Sheetal R. ;
Barbieri, Ettore ;
Terrill, Nicholas J. ;
Knight, Martin M. ;
Gupta, Himadri S. .
ACTA BIOMATERIALIA, 2019, 97 :437-450
[44]   The Secret Life of Collagen: Temporal Changes in Nanoscale Fibrillar Pre-Strain and Molecular Organization during Physiological Loading of Cartilage [J].
Inamdar, Sheetal R. ;
Knight, David P. ;
Terril, Nicholas J. ;
Karunaratne, Angelo ;
Cacho-Nerin, Fernando ;
Knight, Martin M. ;
Gupta, Himadri S. .
ACS NANO, 2017, 11 (10) :9728-9737
[45]  
Kadler KE, 1996, BIOCHEM J, V316, P1
[46]   Collagenolytic Matrix Metalloproteinase Structure-Function Relationships: Insights From Molecular Dynamics Studies [J].
Karabencheva-Christova, Tatyana G. ;
Christov, Christo Z. ;
Fields, Gregg B. .
STRUCTURAL AND MECHANISTIC ENZYMOLOGY, 2017, 109 :1-24
[47]   Dipolar Relaxation of Water Protons in the Vicinity of a Collagen-like Peptide [J].
Karjalainen, Jouni ;
Henschel, Henning ;
Nissi, Mikko J. ;
Nieminen, Miika T. ;
Hanni, Matti .
JOURNAL OF PHYSICAL CHEMISTRY B, 2022, 126 (13) :2538-2551
[48]  
Klein TE, 1999, BIOPOLYMERS, V49, P167
[49]   Observation of angular dependence of T1 in the human white matter at 3T [J].
Knight, Michael J. ;
Damion, Robin A. ;
Kauppinen, Risto A. .
BIOMEDICAL SPECTROSCOPY AND IMAGING, 2018, 7 (3-4) :125-133
[50]   Magnetic Resonance Relaxation Anisotropy: Physical Principles and Uses in Microstructure Imaging [J].
Knight, Michael J. ;
Dillon, Serena ;
Jarutyte, Lina ;
Kauppinen, Risto A. .
BIOPHYSICAL JOURNAL, 2017, 112 (07) :1517-1528