TY - JOUR
T1 - Extended release of proteins following encapsulation in hydroxyapatite/chitosan composite scaffolds for bone tissue engineering applications
AU - Devine, Declan M.
AU - Hoctor, Eilish
AU - Hayes, Jessica S.
AU - Sheehan, Eoin
AU - Evans, Christopher H.
N1 - Funding Information:
This study was supported in part by AIT 's President Seed fund (internal project code P220-594 ), a Marie Curie International Outgoing Fellowship within the 7th European Community Framework Programme (NanoFact 298107,) and the National Institutes of Health ( NIAMS RO1 AR050243 ).
PY - 2018/3/1
Y1 - 2018/3/1
N2 - Researchers describe a new strategy for extending the period of protein release within osseous lesions, by the covalent attachment of the proteins to scaffolds. In this context, they have developed a novel composite scaffold as a delivery vehicle. The composite scaffold was designed to be biomimetic, consisting of hydroxyapatite (HAp) which is similar to the mineral component of bone, in combination with the natural polymer chitosan (CS). HAp is used to enhance the load bearing capacity of the composite utilizing nanocomposite technology to produce a material which mimics the fine structure of natural bone. CS is used as an analog of collagen, which is the polymer phase of bone, and as a molecule to which proteins could be covalently bound.
AB - Researchers describe a new strategy for extending the period of protein release within osseous lesions, by the covalent attachment of the proteins to scaffolds. In this context, they have developed a novel composite scaffold as a delivery vehicle. The composite scaffold was designed to be biomimetic, consisting of hydroxyapatite (HAp) which is similar to the mineral component of bone, in combination with the natural polymer chitosan (CS). HAp is used to enhance the load bearing capacity of the composite utilizing nanocomposite technology to produce a material which mimics the fine structure of natural bone. CS is used as an analog of collagen, which is the polymer phase of bone, and as a molecule to which proteins could be covalently bound.
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U2 - 10.1016/j.msec.2017.11.001
DO - 10.1016/j.msec.2017.11.001
M3 - Article
C2 - 29519440
AN - SCOPUS:85037038532
SN - 0928-4931
VL - 84
SP - 281
EP - 289
JO - Materials Science and Engineering C
JF - Materials Science and Engineering C
ER -