Research output: Contribution to journal › Article › peer-review
Human serum albumin in electrospun PCL fibers : structure, release, and exposure on fiber surface. / Chernonosova, Vera S.; Kvon, Ren I.; Stepanova, Alena O. et al.
In: Polymers for Advanced Technologies, Vol. 28, No. 7, 01.07.2017, p. 819-827.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Human serum albumin in electrospun PCL fibers
T2 - structure, release, and exposure on fiber surface
AU - Chernonosova, Vera S.
AU - Kvon, Ren I.
AU - Stepanova, Alena O.
AU - Larichev, Yurii V.
AU - Karpenko, Andrey A.
AU - Chelobanov, Boris P.
AU - Kiseleva, Elena V.
AU - Laktionov, Pavel P.
PY - 2017/7/1
Y1 - 2017/7/1
N2 - Human serum albumin (HSA) introduced to the fibers produced by electrospinning from HSA and polycaprolactone (PCL) solutions in hexafluoroisopropanol has been studied in terms of its structure, release from the fibers, stability of interaction with basic polymer, accessibility for protease attack, and cellular receptors, as well as dependence of the studied parameters on the protein concentration in fibers. A limited part of the protein leaves the fibers right after soaking with water, whereas the remaining protein stays tightly bound to fibers for a long time because protein nanoparticles are tightly integrated with PCL, as shown by small-angle X-ray scattering. As has been demonstrated, the proteins leave the fibers in complexes with PCL. X-ray photoelectron spectroscopy demonstrates that the protein concentration on the fiber surface is higher than the concentration in electrospinning solution. The surface-exposed protein is recognized by cell receptors and is partially hydrolyzed by proteinase K. The data on pulse protein release, presence of PCL in the protein released from matrixes, overrepresentation of the protein on the fiber surface, and tight interaction of protein with PCL may be useful for rational design of electrospun scaffolds intended for drug delivery and tissue engineering.
AB - Human serum albumin (HSA) introduced to the fibers produced by electrospinning from HSA and polycaprolactone (PCL) solutions in hexafluoroisopropanol has been studied in terms of its structure, release from the fibers, stability of interaction with basic polymer, accessibility for protease attack, and cellular receptors, as well as dependence of the studied parameters on the protein concentration in fibers. A limited part of the protein leaves the fibers right after soaking with water, whereas the remaining protein stays tightly bound to fibers for a long time because protein nanoparticles are tightly integrated with PCL, as shown by small-angle X-ray scattering. As has been demonstrated, the proteins leave the fibers in complexes with PCL. X-ray photoelectron spectroscopy demonstrates that the protein concentration on the fiber surface is higher than the concentration in electrospinning solution. The surface-exposed protein is recognized by cell receptors and is partially hydrolyzed by proteinase K. The data on pulse protein release, presence of PCL in the protein released from matrixes, overrepresentation of the protein on the fiber surface, and tight interaction of protein with PCL may be useful for rational design of electrospun scaffolds intended for drug delivery and tissue engineering.
KW - electrospinning
KW - fiber surface
KW - protein release
KW - SAXS
KW - XPS
KW - REGENERATION
KW - OSTEOGENIC DIFFERENTIATION
KW - PROLIFERATION
KW - MESENCHYMAL STEM-CELLS
KW - NANOFIBROUS SCAFFOLDS
KW - ADHESION
KW - TISSUE ENGINEERING APPLICATIONS
KW - POLYMER NANOFIBERS
KW - BIOMATERIALS
KW - PROTEIN RELEASE
UR - http://www.scopus.com/inward/record.url?scp=85006272129&partnerID=8YFLogxK
U2 - 10.1002/pat.3984
DO - 10.1002/pat.3984
M3 - Article
AN - SCOPUS:85006272129
VL - 28
SP - 819
EP - 827
JO - Polymers for Advanced Technologies
JF - Polymers for Advanced Technologies
SN - 1042-7147
IS - 7
ER -
ID: 10317131