Collagen structure
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Understanding Collagen Structure: Insights from Recent Research
Triple Helical Structure of Collagen
Collagen, the most abundant protein in animals, is characterized by its unique triple helical structure. This structure consists of three parallel, left-handed polyproline II-type helices that form a right-handed bundle 1. The triple helix is stabilized by hydrogen bonds, with two hydrogen bonds for every three residues, a configuration that has been refined to accommodate shorter interatomic contacts than previously thought 2. This helical arrangement is crucial for the mechanical properties and stability of collagen, which are essential for its role in connective tissues 6.
Molecular and Supramolecular Organization
The molecular structure of collagen has been extensively studied, revealing that only two basic types of structures are possible, with detailed work on the coordinates and Fourier transforms of these models 3. Type I collagen, the prototypical fibrillar collagen, forms a supertwisted right-handed microfibril that interdigitates with neighboring microfibrils, creating a quasihexagonal packing topology 7. This intricate arrangement is vital for the structural integrity and function of various tissues, including skin, tendons, and bones 7.
Collagen Types and Their Functions
Collagen is not a single entity but a family of proteins with more than 20 different types identified so far 4. These types are classified based on their ability to form homo- and heterotrimeric assemblies and their participation in supramolecular aggregates. For instance, fibrillar collagens (types I, II, III, V, and XI) form the structural framework of most connective tissues, while type IV collagen forms sheets in basement membranes 5. Other types, such as type VII collagen, play specialized roles in anchoring fibrils and connecting different tissue components 5.
Stability and Degradation
The stability of collagen is influenced by stereoelectronic effects and preorganization, which are critical for maintaining its structural integrity 1. However, collagen is susceptible to degradation by factors such as ultraviolet (UV) radiation. Studies have shown that UV radiation can cause significant changes in collagen's primary and secondary structures, leading to alterations in its mechanical properties 9. The native triple helix structure of collagen provides some resistance to degradation, but once this structure is compromised, the protein becomes more vulnerable to damage 9.
Advances in Collagen-Based Biomaterials
Recent advances in the synthesis and modification of collagen have led to the development of artificial collagen fibrils that mimic the properties of natural collagen. These biomaterials are being explored for various biomedical applications, including skin substitutes, bone and tendon repair, and drug delivery systems 8. The ability to modify collagen to enhance its mechanical strength, thermostability, and resistance to enzymatic degradation is crucial for its use in these applications 8.
Conclusion
Collagen's unique triple helical structure and its ability to form complex supramolecular assemblies are fundamental to its role in the extracellular matrix and connective tissues. Understanding the molecular details and stability factors of collagen is essential for developing advanced biomaterials and therapeutic strategies. Ongoing research continues to uncover the intricate details of collagen's structure and function, paving the way for innovative applications in biomedicine and nanotechnology.
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Most relevant research papers on this topic
Collagen structure and stability.
Understanding collagen structure and stability, along with stereoelectronic effects and preorganization, will guide the development of artificial collagenous materials for biomedicine and nanotechnology.
Highly CitedStructure of Collagen
The triple helical structure of collagen can be constructed with two hydrogen bonds for every three residues, retaining all permissible interatomic contacts and maintaining the observed frequency of 3.0.
Highly CitedThe molecular structure of collagen.
This paper demonstrates that only two basic types of collagen structures are possible, and compares the predicted coordinates and Fourier transforms with observed X-ray diffraction data.
Highly CitedCollagens--structure, function, and biosynthesis.
Different collagen types play crucial roles in tissue structure and function, and understanding their biosynthesis and processing is crucial for understanding collagen-related diseases and developing effective therapeutic treatments.
Highly CitedCollagen family of proteins
Fourteen collagen types form diverse structures in connective tissues, basement membranes, and worm cuticle, playing a crucial role in tissue connectivity.
Highly CitedStructure of Collagen
The structure of collagen is a three-chain coiled-coil, similar to the one found in elastin, with minor modifications.
Microfibrillar structure of type I collagen in situ.
The crystallographic determination of collagen type I's supermolecular structure reveals its molecular packing topology, providing insights into biological processes and diseases like heart disease and cancer.
Highly CitedRecent advances of collagen-based biomaterials: Multi-hierarchical structure, modification and biomedical applications.
Collagen-based biomaterials show promise for biomedical applications, but require modification for improved mechanical strength, thermostability, and resistance to enzymes.
Highly CitedCollagen Structural Hierarchy and Susceptibility to Degradation by Ultraviolet Radiation.
The native collagen triple helix is most sensitive to UV-254nm radiation, affecting tissue remodeling, wound repair, and disease progression.
In Vitro StudyHighly CitedThe structure of fibrous proteins of the collagen-gelatin group.
This study proposes a new, precise configuration for collagen and gelatin, which explains the positions and intensities of x-ray diffraction maxima.
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