Collagen-and hyaluronic acid-based hydrogels and their biomedical applications
Hydrogels have been widely investigated in biomedical fields due to their similar physical
and biochemical properties to the extracellular matrix (ECM). Collagen and hyaluronic acid …
and biochemical properties to the extracellular matrix (ECM). Collagen and hyaluronic acid …
The collagen suprafamily: from biosynthesis to advanced biomaterial development
Collagen is the oldest and most abundant extracellular matrix protein that has found many
applications in food, cosmetic, pharmaceutical, and biomedical industries. First, an overview …
applications in food, cosmetic, pharmaceutical, and biomedical industries. First, an overview …
Applications of fluorine in medicinal chemistry
EP Gillis, KJ Eastman, MD Hill… - Journal of medicinal …, 2015 - ACS Publications
The role of fluorine in drug design and development is expanding rapidly as we learn more
about the unique properties associated with this unusual element and how to deploy it with …
about the unique properties associated with this unusual element and how to deploy it with …
Recent trends in protein and peptide-based biomaterials for advanced drug delivery
Engineering protein and peptide-based materials for drug delivery applications has gained
momentum due to their biochemical and biophysical properties over synthetic materials …
momentum due to their biochemical and biophysical properties over synthetic materials …
Collagen‐based biomaterials for wound healing
S Chattopadhyay, RT Raines - Biopolymers, 2014 - Wiley Online Library
With its wide distribution in soft and hard connective tissues, collagen is the most abundant
of animal proteins. In vitro, natural collagen can be formed into highly organized, three …
of animal proteins. In vitro, natural collagen can be formed into highly organized, three …
Collagen structure and stability
MD Shoulders, RT Raines - Annual review of biochemistry, 2009 - annualreviews.org
Collagen is the most abundant protein in animals. This fibrous, structural protein comprises
a right-handed bundle of three parallel, left-handed polyproline II-type helices. Much …
a right-handed bundle of three parallel, left-handed polyproline II-type helices. Much …
Factors affecting thermal stability of collagen from the aspects of extraction, processing and modification
X Zhang, S Xu, L Shen, G Li - Journal of Leather Science and Engineering, 2020 - Springer
Collagen, as a thermal-sensitive protein, is the most abundant structural protein in animals.
Native collagen has been widely applied in various fields due to its specific physicochemical …
Native collagen has been widely applied in various fields due to its specific physicochemical …
Understanding organofluorine chemistry. An introduction to the C–F bond
D O'Hagan - Chemical Society Reviews, 2008 - pubs.rsc.org
Fluorine is the most electronegative element in the periodic table. When bound to carbon it
forms the strongest bonds in organic chemistry and this makes fluorine substitution attractive …
forms the strongest bonds in organic chemistry and this makes fluorine substitution attractive …
Prolyl 4-hydroxylase
KL Gorres, RT Raines - Critical reviews in biochemistry and …, 2010 - Taylor & Francis
Posttranslational modifications can cause profound changes in protein function. Typically,
these modifications are reversible, and thus provide a biochemical on-off switch. In contrast …
these modifications are reversible, and thus provide a biochemical on-off switch. In contrast …
Collagen structure: new tricks from a very old dog
J Bella - Biochemical Journal, 2016 - portlandpress.com
The main features of the triple helical structure of collagen were deduced in the mid-1950s
from fibre X-ray diffraction of tendons. Yet, the resulting models only could offer an average …
from fibre X-ray diffraction of tendons. Yet, the resulting models only could offer an average …